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Database: UniProt
Entry: C3XQ16_BRAFL
LinkDB: C3XQ16_BRAFL
Original site: C3XQ16_BRAFL 
ID   C3XQ16_BRAFL            Unreviewed;      1609 AA.
AC   C3XQ16;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Malignant fibrous histiocytoma-amplified sequence 1 homolog {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BRAFLDRAFT_67388 {ECO:0000313|EMBL:EEN70037.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739 {ECO:0000313|EMBL:EEN70037.1};
RN   [1] {ECO:0000313|EMBL:EEN70037.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN70037.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN70037.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
CC       {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR   EMBL; GG666451; EEN70037.1; -; Genomic_DNA.
DR   RefSeq; XP_002614028.1; XM_002613982.1.
DR   eggNOG; KOG0619; Eukaryota.
DR   eggNOG; KOG3573; Eukaryota.
DR   InParanoid; C3XQ16; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   CDD; cd00032; CASc; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR033139; Caspase_cys_AS.
DR   InterPro; IPR016129; Caspase_his_AS.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   InterPro; IPR015917; Pept_C14A.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR45752; LEUCINE-RICH REPEAT-CONTAINING; 1.
DR   PANTHER; PTHR45752:SF149; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 39; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF13855; LRR_8; 4.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   Pfam; PF08477; Roc; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   SMART; SM00364; LRR_BAC; 11.
DR   SMART; SM00369; LRR_TYP; 19.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF52058; L domain-like; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01122; CASPASE_CYS; 1.
DR   PROSITE; PS01121; CASPASE_HIS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          768..981
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1343..1465
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   DOMAIN          1515..1604
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
FT   REGION          1493..1520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1609 AA;  183416 MW;  3FD51CD42AE6E40B CRC64;
     MGIDLSTYRA RIGCFSNPGH DSLHCWAEAS CLLVWMVISQ LMLKLAGDVE ENPGPQERYL
     GKTMGTQPMR DEMKREEWKI LGKAQPLWTL DLSNQNHKDL PDEVFELEEL EALKLTYNES
     ISLSNKLVKL TNLKVLCLEN CNLDKLPPVV LKLSHLQVLD ISKNKAISLP KMILKKLKKL
     KVLKLRDCDL VTIGRQIFQQ ESQLEELDLS GNMQIDLPDE LRTLKNIRVL RLNRAGMTTV
     PPAVLELSQL EKLDLSGNKQ IKLSDQLLGL TNLKVLRLSR TEMASVPEVV WKLTHLEELH
     LLSNPLQTLS VKVGQLSRIK RLDLSNCHLR TLPPEVGTLT QLERLKVANN RALQTLPGEL
     WQVTNIKRLD LSNCQLHTLP PEVGTLTQLE WLDLSFNTLQ TLPRELGHVT NIKRLDLSHC
     QLHTLPPQVG KLTHLKWLKV KNNPLQTLPG ELGQVASIKH LDLSNCWLHT LPPEVGTLTQ
     LERLKVANNP LQTLPGELWK VTNIKRLDLS SCWLDTLPPE VGTLTQLEWL SLQGNPLQML
     PKQIGQLTAI KHLNLSFCQL HTLPPEMGTL KQLEWLSLQG NPLQMLPKQV ENLTHIKWMN
     LSHCRLQMLP PEFGKLTQLE RLYLSCNGEL QTLPTRQLTN IKHLDLSNCS LQTLPPEVGE
     LKHVEYLRLS SNPLQKLPPE VRHLTNIKHL DMSNCRLNEL PIEVGTMTQL RQLDLRYNQL
     QMLPVEITQH INLYHLDVRG NPLIRPPAEV CSQGMVAVRQ YFEELESGEA VSTHLKVVVL
     GKELAGKTSL IQTLLSGDSS LTQQEDRTHG VEITQWKPDD NITFEVYDFG GHDAYHLTHQ
     FFLTQDSLHL LTVDLQTYCC TEQDYKNAVG FWLDTLNARV PGAMVTIVCS KSEGSVDIEK
     KTHDIEVKFK EQQDTWKRNL ERQLKIIERA ENQEDLKQQF EDIQQLMTRP LQFKGLCCVS
     SAGPTGLETL TAHVLELAKN TQLFQTHKGI LPQTWVDFEQ RLRNLRDNEA KWLMPADYQQ
     QAQLAGLPTD KLEPVLSYLQ QVGTILRYTD IPELRDFVFH DPPALIEIFK GLFHHNTSDL
     FSTLDIYFTP LDLDKFKSDL DDRGLILKKV MKHLLPPDTP SNIVTSLMQH YDLCFEIDEC
     KTKASDEETR QYMIPWYLHK TMQEKWQHNW PQHVPEEQLQ LMCNIKGFCP RGLFPRFSVG
     IHSLIKDRVD WKDSVMAYRQ DFPVLALCSK PGTDDTYITI ATRGRLAQAD EMWGVVYPLL
     EVLVQLLQKW PGVLYSLHVT CAHCIKARLD NPHQYNLRDQ TADDDRIVRC PKADFRATVS
     TDLVYRPLQQ NKVFQRYKMK TDPRGLALII SNINFMDPET DRQGGNKDLE NIWKICDKLK
     LKAENKDDLT GQEIADTLQE VSERDHSCYD CFVLFLLSHG DEKGVLGTDE DRMISVDSIT
     SSLQLCKSLV GKPKLFFIQA CRGDNFDEGV EYMTTDDIKS PSRVGAEALS ESIMATDSAS
     HQSTTPTASD SGNAKRKTIP TASDRLVMNA TVQGQVAWRD KNTGSPFIQA LADVITEHAD
     TVTLQDMATL VNEKVADYEA DADDDYKQQS EVSHSLRKKL YFFPETAVD
//
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