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Database: UniProt
Entry: A0A2G4T4T5_RHIZD
LinkDB: A0A2G4T4T5_RHIZD
Original site: A0A2G4T4T5_RHIZD 
ID   A0A2G4T4T5_RHIZD        Unreviewed;       439 AA.
AC   A0A2G4T4T5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Endopeptidase S2P {ECO:0000256|ARBA:ARBA00032658};
GN   ORFNames=RHIMIDRAFT_264959 {ECO:0000313|EMBL:PHZ16027.1};
OS   Rhizopus microsporus ATCC 52813.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ16027.1, ECO:0000313|Proteomes:UP000242254};
RN   [1] {ECO:0000313|EMBL:PHZ16027.1, ECO:0000313|Proteomes:UP000242254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ16027.1,
RC   ECO:0000313|Proteomes:UP000242254};
RX   PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA   Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA   Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT   "Lipid metabolic changes in an early divergent fungus govern the
RT   establishment of a mutualistic symbiosis with endobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KZ303843; PHZ16027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4T4T5; -.
DR   STRING; 1340429.A0A2G4T4T5; -.
DR   OrthoDB; 51250at2759; -.
DR   Proteomes; UP000242254; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001193; MBTPS2.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR13325:SF3; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-2 PROTEASE; 1.
DR   PANTHER; PTHR13325; PROTEASE M50 MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE 2 PROTEASE; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   PRINTS; PR01000; SREBPS2PTASE.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        128..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        415..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          58..388
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   439 AA;  48417 MW;  EFDE6B2566E5D901 CRC64;
     MAVIVYAGLK ILSSLTRIAS VDQSQHVKRE LVEPNNGDEQ VFLPMIPGVT LPMSHIGYYL
     LALTVCGLFH EAGHAMASFA EGVPIQSSGM FVMYLYPGAF VNIPDQQLQA LAPFRQLKII
     CAGVWHNLVL YLFASLSLAG GLKLLLILIG WQSLEAQGGV SVVHIRTNSP LATHLPPATL
     IYQLDDTPLT HNIEDWNAFL FKEDGRHALE QGFCVSKTHE NYGDKCCDID DTNPFGRSLN
     ATISCFRSIE TALDKQCLST LPVLASKDIP RCKEASDCHG PEMSCVVPYT PSAAGQVVRI
     YAQIPSWVES EEIDRRRIFI FEGELVDIWE SVKVSILSPR FWILPVSLPH ILELILRYIS
     SFTIALALLN ILPAFKLDGE FALEQLLISF MQPTDASLVT TTRTYRATKQ VQDSIVKVTS
     IVVGFVIVGS LVMGLLSVV
//
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