TAGD_DICDI
ID TAGD_DICDI Reviewed; 1825 AA.
AC Q8T9W1; Q54M85;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Serine protease/ABC transporter B family protein tagD;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease/ABC transporter tagD;
DE Flags: Precursor;
GN Name=tagD; ORFNames=DDB_G0286123;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12456012; DOI=10.1128/ec.1.4.643-652.2002;
RA Anjard C., Loomis W.F.;
RT "Evolutionary analyses of ABC transporters of Dictyostelium discoideum.";
RL Eukaryot. Cell 1:643-652(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ABC transporter
CC superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201)
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peptidase S8
CC family. {ECO:0000305}.
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DR EMBL; AF466309; AAL74253.1; -; Genomic_DNA.
DR EMBL; AAFI02000085; EAL64354.1; -; Genomic_DNA.
DR RefSeq; XP_637863.1; XM_632771.1.
DR AlphaFoldDB; Q8T9W1; -.
DR STRING; 44689.DDB0191427; -.
DR MEROPS; S08.A57; -.
DR PaxDb; Q8T9W1; -.
DR EnsemblProtists; EAL64354; EAL64354; DDB_G0286123.
DR GeneID; 8625460; -.
DR KEGG; ddi:DDB_G0286123; -.
DR dictyBase; DDB_G0286123; tagD.
DR eggNOG; KOG0055; Eukaryota.
DR eggNOG; KOG0058; Eukaryota.
DR HOGENOM; CLU_235711_0_0_1; -.
DR InParanoid; Q8T9W1; -.
DR PhylomeDB; Q8T9W1; -.
DR Reactome; R-DDI-1369007; Mitochondrial ABC transporters.
DR Reactome; R-DDI-159418; Recycling of bile acids and salts.
DR Reactome; R-DDI-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-DDI-382556; ABC-family proteins mediated transport.
DR Reactome; R-DDI-9754706; Atorvastatin ADME.
DR PRO; PR:Q8T9W1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Hydrolase; Membrane; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1825
FT /note="Serine protease/ABC transporter B family protein
FT tagD"
FT /id="PRO_0000330362"
FT TRANSMEM 971..991
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1210..1230
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1304..1324
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1327..1347
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 307..727
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 1075..1358
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1576..1813
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1386..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1518
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 384
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 652
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 1611..1618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 781
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 896
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1018
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1825 AA; 202642 MW; E28160BC78613A3B CRC64;
MKSNTNIRVL LVSGLILIFI FLGIKFEFIN KNNNDKIGIN RKLEFSYFTK NNNNNNNNNF
KQDQLKNKKD KRILLKNEII DTNIKKNIKK NNQKNNNEEI FPNFISRLLK SNDDMEIQQF
TYRKSHYIVQ FKDHINDETR EQFKQFLINT DIVLDEQPYQ SHIVNYIPHD SFLVLMNDEQ
SNLLSSKEWV SWIGEFEPSN KIHLNYNEKS IGLPVYIKLS DSTNSLIQRW ENTLNSILTS
YNSKVKLTLI NQKKLKSIVY CNDESSSQSS CSLVSSEKLV YQWISEQSES NYIERSEKFQ
TANRLSPKAI FGTKDTLVNN DRIDIPLRGK GQILSIADTG LDGSHCFFSD SNNPIPYNSV
NLNHRKVVTY IGSLHDNEDY VDGHGTHVCG SAAGAPEDSS LAISSFSGLA TDAKIAFFDL
ASDPSNNEPV PPEDYSQLYQ PLYNAGARVH GDSWGSLSIQ GYLGSYSDDA GSIDDFLYTH
PDFIILRAAG NNEQYSSLLS QATAKNVITV GAEQTTHESY TTDALEYSNF ETVAKSTLNS
LCQSFDDKYC TYTTAQCCTE YSTVKGLSGC CTSYIKNSYA SIFSSQPELY NENNICSFSS
KGPTHDGRLK PDIVAPGQYI TSARSNGANT TDQCGDGSLP NTNALLSESG TSMATPLATA
ATTILRQYLV DGYYPTGSIV ESNKLQPTGS LLKALMINNA QLLNGTFPLS STNTNPSNAV
FDTFAGANFV QGWGSLRMSE WLYVESSGVK PKPSRWVGIG ELGKDKKASN WKEYSLSTGQ
NVSYCFTYKP SSSGSNSGGI PRIVATLVWT DPPSYSGAKL NLVNNLDLTM TNTESEFIFY
SNSGGSSYNG TKGTTLPLQD SINNVEGIIY TPINTKSEIS FRFIIAGTNI PIGPQNFSFV
FHGENGEFDW ADSCMQCNPD DTQPCFIENG VGSQTCGDDY LWGRCLVQSC NNNYNYNSIS
DKCSKFLSYN YIVIIVAGGT MSLIITVLIL IKYMEYKENG NKFSLKEFFS GVLGTGKNVS
GGGKGGSGGS GSGSGTLKDG TIDDGTGIHV RPKPKDAPVT PPDLYSLLSP FIIEITISTA
CSLVATAASI LQPYYIGQII QDIPTTKGIG DLRDQFIIIF LLALLEFVFS TISSWISGIV
NEKMVMRLQN KVFRALIAQD MGFFQKNSAA VLMNVLIVDT PMLRSSLTGI LLSVSVGICK
FVGSLVFIFT ISWKLSLAFF ATVPVLAIVT QVQSKFTKRL TRRLLFHNSK ASQHGQESMV
NMHVVSNYCK QDREIAKYSE QLMMVFQISR RLIINNTFAA SIKWLMVESL AFIILYFGAY
LAIQKQFTVG LLVSFSLYIG YVIDSSTTLF GVYSSYVQCL ASATRVFLIL RSAPRKRTTL
EEEELDNIID TNQDNNNNNN NDDISDSSSD DDDDNNNNKN SKNNKTKSGE SDDSSSEDAE
YKKNKNKRNN GKMTTKLSNS PPLVGEGIDN NNNNNNDNNI NDDNNQQDPN NNNNEIDDDG
DDDGDDDDEG EDENNNNNNN DDPNDNNGIE MLTEKQLRKR KRQMKKEFYK KTGISCLELN
LIPSAYTELT ECRGEIEFKN VSFCYPSRAD VGVLYNIDLK FESGKCYGLV GPSGSGKSTL
LELISRFYSL HPSGGKIYMD GIDIAKIRPS NLRSFVTNVH QHPFLFDATI SENIGYALDN
PTQEDIIEAA KLANAHEFIQ SLPKQYDTML TDGGNLSGGQ KKRIAVARAI CAKRKIMLLD
EITAELDPES EEAINKSIKV LTRGHTVVMV AHKVAAVRDC DKIFVLDKGQ IVEQGTHNQL
MAKKGKYYRM FAFSEDDDYA PLLVL
