MCA1B_NEUCR
ID MCA1B_NEUCR Reviewed; 426 AA.
AC Q7S4N5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Metacaspase-1B;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=casB; ORFNames=NCU02400;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Involved in cell death (apoptosis). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
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DR EMBL; CM002242; EAA30484.2; -; Genomic_DNA.
DR RefSeq; XP_959720.2; XM_954627.2.
DR AlphaFoldDB; Q7S4N5; -.
DR SMR; Q7S4N5; -.
DR STRING; 5141.EFNCRP00000003268; -.
DR EnsemblFungi; EAA30484; EAA30484; NCU02400.
DR GeneID; 3875867; -.
DR KEGG; ncr:NCU02400; -.
DR VEuPathDB; FungiDB:NCU02400; -.
DR HOGENOM; CLU_029389_0_2_1; -.
DR InParanoid; Q7S4N5; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR SUPFAM; SSF52129; SSF52129; 1.
PE 3: Inferred from homology;
KW Apoptosis; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Zymogen.
FT PROPEP 1..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000333662"
FT CHAIN ?..426
FT /note="Metacaspase-1B"
FT /id="PRO_0000333663"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /evidence="ECO:0000250"
FT ACT_SITE 273
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 47287 MW; E43EB0862AEBD97B CRC64;
MSGYPGAGYN GGGYVPPPQP QYGGYYPPQP AYNAYQQPPP QQQQYMVYHQ PSPGPQQHQH
WNPQQQTPAP QGYGNPPNSH YGRPEANMPT VNSNSYAHGN HQAPPPPPQA PQQFGYGAPA
DYAFRYSQCN GRHKALLIGI NYFGQRGQLR GCINDVRNMS SYLVEHFRYK REDMVILTDD
QQNPMSQPTK QNILRAMHWL VKDARPNDSL FFHYSGHGGQ TKDLDGDEED GYDEVIYPVD
FRQVGHITDD EMHRIMVRPL QAGVRLTAIF DSCHSGTALD LPYIYSTQGI LKEPNLAKEA
GQGLLGAISS YSQGDLYGVA NNIMGIFKKA TGGNDAHART LATKTSPADV VMFSGSKDDQ
TSADATIASQ ATGAMSWAFI NALKKNPQQS YVQLLNSIRD ELQMRYTQKP QLSCSHPLDT
NLLFVM