ID A0A3Q1J5A3_ANATE Unreviewed; 775 AA.
AC A0A3Q1J5A3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 2 {ECO:0000256|RuleBase:RU365006};
DE AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit {ECO:0000256|RuleBase:RU365006};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000025458.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000025458.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365006}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000256|RuleBase:RU365006}.
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DR AlphaFoldDB; A0A3Q1J5A3; -.
DR STRING; 64144.ENSATEP00000025458; -.
DR Ensembl; ENSATET00000025876.2; ENSATEP00000025458.2; ENSATEG00000017644.2.
DR GeneTree; ENSGT00910000144260; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR PANTHER; PTHR45922; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 2; 1.
DR PANTHER; PTHR45922:SF1; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 2; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 243..368
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 408..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 87659 MW; E134AAA155CF38AC CRC64;
MTSIIKLTAV SGVQEESALC YLLQVDEFRF LLDCGWDENF SMDIIDAMKR YVHQVDAVLL
SHPDPIHLGA LPYAVGKLGL NCTIYATIPV YKMGQMFMYD LYQSRNNSED FTLFTLDDVD
SAFDKIQQLK YSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEV VYAVDFNHKR
EIHLNGCTLE SISRPSLLIT DSFNATYVQP RRKQRDEQLL TNVMETLRGD GNVLIAVDTA
GRVLELAQLL DQIWRTKDAG LGVYPLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
NPFQFRHLTL CHSLADLARV PSPKVVLCSQ PDLESGFSRE LFIHWCQDSK NSIILTYRTT
PGTLARYLID NPGEKMLDLE VRKRVKLEGK ELEEYLEREK IKKEAAKKLE QEKEVDVDSS
DESDMDDDLD QPAAVKNKHH DLMMKAEGSR KGSFFKQAKK SYPMFPAHEE RIKWDEYGEI
IRLEEFLVPE LQATEEEKSK LESGLTNGDE PMDQDLSVVP TKCISSVESL EIRARVTYID
YEGRSDGDSI KKIINQMKPR QLAIVHGPPE ASLDLAESCK AFSKDIKVYT PKLQETVDAT
SETHIYQVRL KDSLVSSLQF CKAKDTELAW IDGVLDMRVI KVDTGVMLEE GMKEEAEDGD
LAMDIAPELD IDHNTTAAAA QRAMKNLFGE DEKELSEESD VIPTLEPLPP HEIPGHQSVF
INEPRLSDFK QVLLREGIQA EFVGGVLVCN NMVAVRRVSV LPPVFISRIK NPKGI
//
