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Database: UniProt
Entry: N1PZK2_DOTSN
LinkDB: N1PZK2_DOTSN
Original site: N1PZK2_DOTSN 
ID   N1PZK2_DOTSN            Unreviewed;       839 AA.
AC   N1PZK2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EME47614.1};
GN   ORFNames=DOTSEDRAFT_146416 {ECO:0000313|EMBL:EME47614.1};
OS   Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS   fungus) (Mycosphaerella pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=675120 {ECO:0000313|EMBL:EME47614.1, ECO:0000313|Proteomes:UP000016933};
RN   [1] {ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA   de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA   Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA   Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA   Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA   Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA   Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA   Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA   Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT   "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT   Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT   but also signatures of common ancestry.";
RL   PLoS Genet. 8:E1003088-E1003088(2012).
RN   [2] {ECO:0000313|EMBL:EME47614.1, ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010624}.
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DR   EMBL; KB446536; EME47614.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1PZK2; -.
DR   STRING; 675120.N1PZK2; -.
DR   EnsemblFungi; EME47614; EME47614; DOTSEDRAFT_146416.
DR   eggNOG; KOG1137; Eukaryota.
DR   HOGENOM; CLU_009673_2_1_1; -.
DR   OMA; CKQHITL; -.
DR   OrthoDB; 169081at2759; -.
DR   Proteomes; UP000016933; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd16292; CPSF3-like_MBL-fold; 1.
DR   Gene3D; 3.40.50.10890; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR022712; Beta_Casp.
DR   InterPro; IPR021718; CPSF73-100_C.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR011108; RMMBL.
DR   PANTHER; PTHR11203; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR FAMILY MEMBER; 1.
DR   PANTHER; PTHR11203:SF11; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 3; 1.
DR   Pfam; PF10996; Beta-Casp; 1.
DR   Pfam; PF11718; CPSF73-100_C; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   SMART; SM01027; Beta-Casp; 1.
DR   SMART; SM01098; CPSF73-100_C; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016933}.
FT   DOMAIN          39..261
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   DOMAIN          273..404
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   DOMAIN          554..837
FT                   /note="Pre-mRNA 3'-end-processing endonuclease
FT                   polyadenylation factor C-term"
FT                   /evidence="ECO:0000259|SMART:SM01098"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..715
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  92957 MW;  CD74A46594A8D416 CRC64;
     MATNKRSRRE ISAQELQDEP VDPSDEFMFL ALGGGNEVGR SCHIVQYKGK TVMLDAGIHP
     SYEGLGALPF YDEFDLSTVD LLLITHFHQD HSASLPYVLA KTDFHGKVFM THPTKAIYKW
     TTQDAVRVHN THTPASSTSG TDGYVSQLYT EQDILSTLPM IQTISFNTTH SHNGIRFTPY
     PAGHVLGACM YHIEIAGLNI LFTGDYSREI DRHLIPATIP PNVKIDCLIT ESTFGISTRE
     PRQERENQLM KSVTNILNRG GRVLMPTTAV GNTQELLLIL EDYWQRHEEY RRFPIYYASG
     LARKVMVVYQ TYVDNMNDRI KAKFQASAAA AGDGGAAGPW DFQFVRALKG VDRFEDVGGS
     VVLASPGMLQ NGPSRALLER WAPDPKNGVV ITGYSVEGTM AKQIMLEPDS IAAVTNRTAN
     MSLGKRAGAE EQQMIPRRCT VQEFNFAVHV DGQENRDFIE ETGAPVVILV HGEKHNMGRL
     KSRLLSLKKM KVYSPANCEE VRIPFRQEKI ARVVGRLANQ IQPPAIPPSP PDSDDEGEEG
     SDSKRVKAEE AQDQAQIVSG VLVQNDFKLS LMAPEDLKEY AGLTTTTLVC RQRIKLASAS
     VGLIQWALEG TFGTVSITTP PKHESTNGNW SNETANEEVP RHTITTFDIM GGAVHVNYKT
     GGDLELEWEG NATNDSIADA VMAVLLTVET SPAAVKQSSQ LHDHSHHDKK SNGNLKRNPH
     ANLTAEEKLN RLFMFLEAQF GEEAITPIEK PKRLEPAATH GETAEVEMYE TTEEKMEARE
     VARLHAAGVP VPGLEIRVDQ HRAKVWLEKL EVECANSALK ARIKAVVERA VEVVAPLWQ
//
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