ID A0A3B5AA69_9TELE Unreviewed; 791 AA.
AC A0A3B5AA69;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000017645.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000017645.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B5AA69; -.
DR STRING; 144197.ENSSPAP00000017645; -.
DR Ensembl; ENSSPAT00000017919.1; ENSSPAP00000017645.1; ENSSPAG00000013284.1.
DR GeneTree; ENSGT00910000144260; -.
DR Proteomes; UP000261400; 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 RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 243..372
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 413..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 89592 MW; C3044A218B396D15 CRC64;
MTSIIKLTAV SGVQEESALC YLLQVDEFRF LLDCGWDENF SMDIIDAMKR YVHQVDAVLL
SHPDPIHLGA LPYAVGKLGL NCTIYATIPV YKMGQMFMYD LYQSRNNSED FTLFTLDDVD
CAFDKIQQLK YSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI IYAVDFNHKR
EIHLNGCTLE SISRPSLLIT DSFNAAYVQP RRKQRDEQLL TNVMETLRGD GNVLIAVDTA
GRVLELAQLL DQIWRTKDAG LGAYPLALLN NVSYNVVEFS KSQTSLLVEW MSDKLMRCFE
DKRNNPFQFR HLTLCHSLAD LARVPSPKVV LCSQPDLESG FSRELFIQWC QNAKNSIILT
YRTTPGTLAR YLIDNPGEKM LCLEVRKRVK LEGKELEEYL EKEKIKKEAT KKLEQAKEVD
VDSSDESDMD DDLDQPAAVK SKHHDLMMKS EGSRKGSFFK QAKKSYPMFP THEERIKWDE
YGEIIRLEEF LVPELQATEE EKSKLESGLT NGDEPMDQDL SVVPTKCISN IENLEIRARI
TYIDYEGRSD GDSIKKIINQ MKPRQLVIVH GPPEASLDLA ESCKAFSKDL KVYTPKLQET
VDATSETHIY QVRLKDSLVS SLQFCKAKDT ELAWIDGVLD MRVVKVDTGV MLEEGVKEEA
EDGELAMDIT PDLGIDQNAT AVATQRAMKN LFGEDEKEFS EESDVIPTLE PLPPHEIPGH
QSVFINEPRL SDFKQVLLRE GIQAEFVGGV LVCNNMVAVR RTEAGRIGLE GCLCDDYYKI
RELLYQQYAV V
//
