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NM111_NEUCR
ID   NM111_NEUCR             Reviewed;        1026 AA.
AC   Q7S9D2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Pro-apoptotic serine protease nma111;
DE            EC=3.4.21.-;
GN   Name=nma111; ORFNames=NCU05200;
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: Nuclear serine protease which mediates apoptosis.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA32963.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CM002239; EAA32963.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_962199.2; XM_957106.3.
DR   AlphaFoldDB; Q7S9D2; -.
DR   SMR; Q7S9D2; -.
DR   STRING; 5141.EFNCRP00000004971; -.
DR   EnsemblFungi; EAA32963; EAA32963; NCU05200.
DR   GeneID; 3878338; -.
DR   KEGG; ncr:NCU05200; -.
DR   HOGENOM; CLU_003212_0_0_1; -.
DR   InParanoid; Q7S9D2; -.
DR   OMA; CVFDNHE; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
DR   GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; IEA:EnsemblFungi.
DR   GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IEA:EnsemblFungi.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR025926; PDZ-like_dom.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF12812; PDZ_1; 2.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50156; SSF50156; 3.
DR   SUPFAM; SSF50494; SSF50494; 2.
PE   3: Inferred from homology;
KW   Apoptosis; Hydrolase; Nucleus; Protease; Reference proteome; Repeat;
KW   Serine protease.
FT   CHAIN           1..1026
FT                   /note="Pro-apoptotic serine protease nma111"
FT                   /id="PRO_0000320357"
FT   DOMAIN          305..377
FT                   /note="PDZ 1"
FT   DOMAIN          883..955
FT                   /note="PDZ 2"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..272
FT                   /note="Serine protease"
FT   COMPBIAS        14..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        151
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        233
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1026 AA;  113311 MW;  B44B2E795EDDEA2C CRC64;
     MNGTSPVARS KRKEPPQYSS DGRLAKHHRT NGDIDMSSAD ANTPTEDFDG HYEEEPRHVL
     PLAPGADTAE WQATIENVVR NVVSIRFCQT CSFDTDPALT SEATGFVVDA ERGYILTNRH
     VVGSGPFWGY CIFDNHEEVD AYPVYRDPVH DFGILKFDPK AIKYMPVAAL PLRPDLARVG
     IEIRVVGNDA GEKLSILSGV ISRLDRNAPE YGDGYSDFNT CYYQASAAAS GGSSGSPVVN
     KDGFAVALQA GGRADGASTD YFLPLDRPLR ALKCLQEGKP ITRGDIQCQF VLKPFDECRR
     LGLTPEWEAQ VRKAFPKETN MLVAEIILPE GPSHKKLEEG DVLIKVNGKL LTQFIPLEET
     LDSSVGQTVK LMLLRGGEEV EVEIEVGDLH QITPDRFVSV SGGSFHNLSY QQARLYGVAC
     KGVYVCEAGG SFRFDNNENG WIIQSIDQKE TPDLDTFIEV MKGIPDKARV VITYKHLRDM
     HTLHTTVIYV DRHWAKKMKL AVRNDKTGLW DFSNLSDALP AVAPVPRKAS FIQLENTSHP
     AVADLVKSFV HVSVTMPVKL DGFPKNRKWG MGLVIDAEKG LVIISRAIVP YDLCDITITI
     ADSIVVEGKV VFLHPLQNYA VIQYDPKLVD APVRSAKLSS EMISQGASTY FIGYNRIGRI
     VHTATTVTEM FAVTIPANSG APRYRAVNVD AITVDTNLSG QCGSGVLVAQ DGTVQALWLT
     YLGERNPSSH RDEEYHLGLA TPTLLPVISQ LQQGITPKLR LLSCEFRAIQ MSQARIMGVS
     EEWIQKVSLV NTAHHQLFLV TKRTYERNEP AGDHLKEGDI LLTLNNQLIT KISELDVMYS
     HDYLDAVIVR NTKELHIKLP TVAADDAETD HAISFCGAIL HRPHLAVRQQ ISKLFSEVYV
     SARTRGSPAY QYGLAPTNFV THVNGKRTPD LKSFLDAVVG IPDNTYFRLK CMTFDSVPWV
     VTMKKNEHYF PTTELIKDPS EPLTGWRRIT YEGGKKIEGE GHEGVGVAVL GEDQGEGGEG
     DVDGCC
 
 
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