ID J9FRH7_9SPIT Unreviewed; 438 AA.
AC J9FRH7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Hemoglobinase-type cysteine proteinase {ECO:0000313|EMBL:EJY80671.1};
GN ORFNames=OXYTRI_21939 {ECO:0000313|EMBL:EJY80671.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY80671.1};
RN [1] {ECO:0000313|EMBL:EJY80671.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY80671.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY80671.1}.
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DR EMBL; AMCR01007543; EJY80671.1; -; Genomic_DNA.
DR AlphaFoldDB; J9FRH7; -.
DR EnsemblProtists; EJY80671; EJY80671; OXYTRI_21939.
DR OrthoDB; 2951493at2759; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd21115; legumain_C; 1.
DR Gene3D; 1.10.132.130; -; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR048501; Legum_prodom.
DR InterPro; IPR046427; Legumain_prodom_sf.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR12000:SF42; LEGUMAIN; 1.
DR Pfam; PF20985; Legum_prodom; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..438
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003822723"
FT DOMAIN 382..428
FT /note="Legumain prodomain"
FT /evidence="ECO:0000259|Pfam:PF20985"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 179
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 438 AA; 48843 MW; 72C2EBEE385A793D CRC64;
MYKLTLAIAA LLGYVQAIDH WAVIVAGSNG FWNYRHQADA CHAYQIMKKN GIPDSNIITM
IYDDVANDPE NPFPGKIFNK PNGQDVYAGC NIDYKGASVN PTNFLNILKG DAAGVSGGNG
KVLKSTADSK VFVFFADHGA PGLIAFPNEY LYANDLNSAF NYMHDNKMYN ELVFYLEACE
SGSMFEGILK DNLNIYAITA ANADESSWGT YCYPDDQVNG THINSCLGDL FSVNWMEDSD
AQNVHTESLE TQFQKILKTT DKSHVMRYGQ QTFTKEPIGN FQGNFNDAEI TDKAGNFFQK
LLKQAKREVT DAAPVDAKKH ISAVHSRDAK LHHLYSTLQT KPGHKITIDL SSELNARMRS
DHVFEDLVPT TLRASSETIR PRNFECLKQA VNTYEKHCGK FSDYDLKYVR NLVILCETAP
SQQATELTTA KIQDACSH
//
