ID A0A0D3KRH4_EMIH1 Unreviewed; 961 AA.
AC A0A0D3KRH4;
DT 05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 1.
DT 28-JAN-2026, entry version 5.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|RuleBase:RU003874};
OS Emiliania huxleyi (strain CCMP1516).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=280463 {ECO:0000313|EnsemblProtists:EOD38359, ECO:0000313|Proteomes:UP000013827};
RN [1] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [2] {ECO:0000313|EnsemblProtists:EOD38359}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (OCT-2024) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650,
CC ECO:0000256|RuleBase:RU003874}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005790788.1; XM_005790731.1.
DR AlphaFoldDB; A0A0D3KRH4; -.
DR STRING; 2903.R1FXV3; -.
DR PaxDb; 2903-EOD38359; -.
DR EnsemblProtists; EOD38359; EOD38359; EMIHUDRAFT_466893.
DR GeneID; 17283629; -.
DR KEGG; ehx:EMIHUDRAFT_466893; -.
DR eggNOG; ENOG502QS7I; Eukaryota.
DR HOGENOM; CLU_005314_3_0_1; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR CDD; cd17928; DEXDc_SecA; 1.
DR FunFam; 3.90.1440.10:FF:000003; Preprotein translocase SecA subunit; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR020937; SecA_CS.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR044722; SecA_SF2_C.
DR InterPro; IPR011116; SecA_Wing/Scaffold.
DR InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR InterPro; IPR036670; SecA_X-link_sf.
DR NCBIfam; TIGR00963; secA; 1.
DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
DR PRINTS; PR00906; SECA.
DR SMART; SM00957; SecA_DEAD; 1.
DR SMART; SM00958; SecA_PP_bind; 1.
DR SUPFAM; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003874};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003874};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU003874};
KW Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW Signal {ECO:0000256|SAM:SignalP};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Translocation {ECO:0000256|ARBA:ARBA00023010,
KW ECO:0000256|RuleBase:RU003874};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003874}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..961
FT /note="Protein translocase subunit SecA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044291909"
FT DOMAIN 66..768
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 152..312
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 84..111
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 961 AA; 103136 MW; 004C9AEB0EF28B54 CRC64;
MLAALASLLV GGSTAYLPLA PAVRVCTHQR PAVASPTRTA SAAMGVLDQV SEAIRGGGEQ
ASDSKSDPKT AAFTAANDRT VMAYTERVAR INDLEDEIEA LEDEALAAKT AEFRKRLAAG
ETEEELLEEA FAVVREAAWR TLDLRHYDVQ LVGAMALNDG KLAQMGTGEG KTLVATGAVY
LNALSGKGAM VVTVNDYLAR RDAEGMGQVY AFLGLSVGLV QSGSDTAARR EAYASDVTYV
TNSELGFDYL RDNLAVTAEE VVLRRELNYC VVDEGDSVLI DEARVPLIIS GKTDAPVDKF
GAASKLAAVL ERGIHYDVFE KEQTVSLTDK GTRDCEKALA VGDLYEPTNP WASYVSNALK
AKELFVKERS YLVQGGEAVI IDEFSGRVME GRRWGDGLHQ AVEAKEGLTV QPETEVVASV
TYQSLFRRFR KLSSMSGTAL SEAEEFATIY GLDVVDVPPV LPSLRSDIPD SVFKTTRGKS
NAALAELLSL RRSGRPILVG TTSVEASQVF SDKLTELGVK HEVLSAAPEA AQREAEVVAQ
AGREGSVTIS TNMAGRGTDI LLGGNPAFMA RLYLRTAFAA AAGLSGVTPP RDGFFPRAVS
EEAEAAVGRA AARFAQSRAA AAADDDAEGH ERAELAAPDE GCSPWHFRGG FPERRLLAVA
ASSAAVFEES VEDEAREALE AVGEEFAEEL APEKERVLQA GGLHVIGTNL HDSRRIDGQL
RGRAGRQGDP GSTHFFLSLE DRIFRLFGGD KIKGLLDFMR ISEDQPLESG QVQRVVEETQ
AKVLAVQRED TYRTRAAVLR GSADEVLDTL AAHAAGTASD ILKSNLDASG AEATLAKLQQ
FFPAVPLTAA DLEGDGAEER AHAAVQEALR AKAAELDSVR PGLAVESGRF LALTQTDTLW
KAHMKAMGYV KDFAGLKAYS GTDPIQVYRE EGLRLYEAMQ TSLRQNTAFS FFQYQPRSKG
A
//
