PCH2_CAEEL
ID PCH2_CAEEL Reviewed; 424 AA.
AC Q09535;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Putative pachytene checkpoint protein 2;
GN Name=pch-2; ORFNames=F10B5.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Plays a key role in chromosome recombination during meiosis.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. PCH2 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z48334; CAA88312.1; -; Genomic_DNA.
DR PIR; T20692; T20692.
DR RefSeq; NP_495711.1; NM_063310.6.
DR PDB; 4XGU; X-ray; 2.30 A; A/B/C/D/E/F=1-424.
DR PDBsum; 4XGU; -.
DR AlphaFoldDB; Q09535; -.
DR SMR; Q09535; -.
DR BioGRID; 39642; 7.
DR DIP; DIP-26661N; -.
DR STRING; 6239.F10B5.5; -.
DR EPD; Q09535; -.
DR PaxDb; Q09535; -.
DR PeptideAtlas; Q09535; -.
DR EnsemblMetazoa; F10B5.5.1; F10B5.5.1; WBGene00008641.
DR GeneID; 174313; -.
DR KEGG; cel:CELE_F10B5.5; -.
DR UCSC; F10B5.5; c. elegans.
DR CTD; 174313; -.
DR WormBase; F10B5.5; CE01547; WBGene00008641; pch-2.
DR eggNOG; KOG0744; Eukaryota.
DR GeneTree; ENSGT00940000170021; -.
DR HOGENOM; CLU_028208_1_0_1; -.
DR InParanoid; Q09535; -.
DR OMA; HCEKLMQ; -.
DR OrthoDB; 1036414at2759; -.
DR PhylomeDB; Q09535; -.
DR SignaLink; Q09535; -.
DR PRO; PR:Q09535; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008641; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044539; Pch2-like.
DR PANTHER; PTHR45991; PTHR45991; 1.
DR Pfam; PF00004; AAA; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Meiosis; Nucleotide-binding; Reference proteome.
FT CHAIN 1..424
FT /note="Putative pachytene checkpoint protein 2"
FT /id="PRO_0000084790"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:4XGU"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:4XGU"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:4XGU"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 290..303
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 324..341
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 367..378
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 390..397
FT /evidence="ECO:0007829|PDB:4XGU"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:4XGU"
FT HELIX 405..423
FT /evidence="ECO:0007829|PDB:4XGU"
SQ SEQUENCE 424 AA; 48023 MW; 1472788F7BCDC88F CRC64;
MHEPMKTLKN IHAEIRICQK FPKSTVQKRF SEFEELIKAA SKNARNWKPI SSVELFQGDS
SLNELFEKLV IGTCELRDGE LFENVNDLTI NPSNIHVYKL HKDGPLSQNI GDDDGDESII
GSQLWQLPCV EFDSIWENLI YDSNLKNEVM SYVAALARLS EKHVNTKIIN VNRLILLTGP
PGTGKTSLCK GLAQHLSIRM NDKYSKSVML EINSHSLFSK WFSESGKLVQ KMFDQIDELA
EDEKCMVFVL IDEVESLGMC RESSSSRSEP SDAIRAVNAL LTQIDRIRRR DNVLILCTSN
LESTLDKALV DRADIVKNVG QPSDFARYSM LKSSIMELAR IGVVIDNEVH TDYWPQDICD
TKAPRNEFTE ILFKIAQEAR GLSGRAISML PTLVYSKSPE ETITLPNCMN LFLEAVKERL
SRNN
