ID   D2VB62_NAEGR            Unreviewed;       833 AA.
AC   D2VB62;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Abc transporter B family protein {ECO:0000313|EMBL:EFC45741.1};
GN   ORFNames=NAEGRDRAFT_79279 {ECO:0000313|EMBL:EFC45741.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC45741.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC45741.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; GG738861; EFC45741.1; -; Genomic_DNA.
DR   RefSeq; XP_002678485.1; XM_002678439.1.
DR   AlphaFoldDB; D2VB62; -.
DR   STRING; 5762.D2VB62; -.
DR   EnsemblProtists; EFC45741; EFC45741; NAEGRDRAFT_79279.
DR   GeneID; 8858965; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_79279; -.
DR   InParanoid; D2VB62; -.
DR   OrthoDB; 6914at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          220..647
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        229
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        285
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        590
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   833 AA;  92902 MW;  EA41269D4C4E355F CRC64;
     MYNLFTQNEK RRDMNRFLHE SNPFLLNEPL LSSTLNHQRN IQQEDETQFF SVLLKVKDIQ
     KFKKENTNLN IQPMAKNVIS TRMDMDSIQS LLGKDYIEWI GQIDPIFKFD IQDFMENKQE
     TVELLIQFAS GISNEMKRMM EIFETQFGVS LLRIEKQNLM LLTVPRRYAL GVSYEISKDS
     SVIWIEPKQE ISLTNKFSKS IIDDGSERIQ ERVNFGGLTG EGETVTVVDG SFDVTSCFFA
     DPNVPVTQFK TYKEGMKLTS QQVNSHRKIK AYYAFVDNRT RDSDHGSHVA GSVAGNSIYS
     NSIGDTLVSD YNGIAPDSKM VFIQLGCTSP VCISENGEKF TSSPGSLFPP SDPYNFFSFS
     KEIANSRVQT NSWGGGSSYN YYASSTDEYI FNNKDMVTLF AAGNSGRSGF KTIGGQAHAK
     NVITVGASHN SFGARTVQYA NLTSSTNSVV REYIVAVLQC SPYSTKYINQ CTYFNDLNNI
     VDACDESGYC AKGTMSVSTG SCGCAIGGVG QLYCGRCVYP SLAVKDIQPD SVTSFSSRGP
     TMDGRIKPDI MAPGDQIISV RSYPTLDDVG TQCSQRKNLI DHVTAKRGTS MATPTLAGLT
     AIVRQYFRDG YYVDGVKNAK IAFNPSASLV KATMINSAVD LASLSEDTQF LEKLAPRNWN
     STRYQGFGKV QIDNVFQFGK SERKLWIGRT ENIQNIAQLS NVETEFGDPV LSSVEDEHVY
     YIAPTNANLP MKNVKITLVW SDYPSNPLSR LNIVNNLDLE VNVFRDVIFG NSQLYGLSQD
     NMARDTLNNV EQVWLDSTDH GVVIRVYAEY LFVPQSYSLV VSGDNVSMHL LKE
//