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Database: UniProt
Entry: A0A452H5P5_9SAUR
LinkDB: A0A452H5P5_9SAUR
Original site: A0A452H5P5_9SAUR 
ID   A0A452H5P5_9SAUR        Unreviewed;       719 AA.
AC   A0A452H5P5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Zinc finger CCHC domain-containing protein 8 {ECO:0000256|ARBA:ARBA00022379};
DE   AltName: Full=TRAMP-like complex RNA-binding factor ZCCHC8 {ECO:0000256|ARBA:ARBA00032546};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000009979.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000009979.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000256|ARBA:ARBA00004642}.
CC   -!- SIMILARITY: Belongs to the ZCCHC8 family.
CC       {ECO:0000256|ARBA:ARBA00007497}.
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DR   AlphaFoldDB; A0A452H5P5; -.
DR   STRING; 38772.ENSGAGP00000009979; -.
DR   Ensembl; ENSGAGT00000011457.1; ENSGAGP00000009979.1; ENSGAGG00000007842.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR006568; PSP_pro-rich.
DR   InterPro; IPR001878; Znf_CCHC.
DR   PANTHER; PTHR13316:SF0; ZINC FINGER CCHC DOMAIN-CONTAINING PROTEIN 8; 1.
DR   PANTHER; PTHR13316; ZINC FINGER, CCHC DOMAIN CONTAINING 8; 1.
DR   Pfam; PF04046; PSP; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00581; PSP; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          226..241
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          406..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          43..70
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        406..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..494
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  79809 MW;  16774B862ED5BCA2 CRC64;
     MAAEVDFGDR ELFEQLDGDE AAAPTAQPLH TRFEEDVELE EAGEALRERL RDSEEMVRQL
     RSENQELRRK LKILTRPSGL SVDSSKLDGP LLQILFMNNI ISKQYHQEIE DFISSLVQKY
     EEQQKAEPER THFNVKPQPS SILLEEDHKV TSSNTIKKIK EAFSVVGSVL YFTNFCLDKL
     GQPILNENPQ LTEGWEIPKY QQVFSQILSL DGQEIQVKAK RPKPHCFNCG SEEHQMKECP
     KPRNATRISE KRREFMEACG EASNQNFQQR YHADEVEERF GKFKPGIISE ELQDALGVTD
     KSLPPFIYRM RQLGYPPGWL KEAELEDSGL ALYDGKDATG GDTEDERPYQ QNKCVTYDVS
     KLINYPGFNM STPSGISDEW RIFGSIPMQP SQQKDIFASY LSNFRAPSPK SSNKRSAYPS
     SSHNSKKVKG DNSAVSVADM DMDSDLEMPH SSLAYDSFQF QPPLPPGSPS IATPPPLPRG
     TPPCTPPNFT SPLPPAPTAS LHRNSPASTP SSDSAQPGVG DSAMDEDTLT LEELEEQQRL
     IWAALEQADS TNSDSDIPAE TPLTGNSVTS SPSRNELDIV PEGRTSEKLV GMEIGISDTS
     MQISRNEHSK SDPNSGDGLL DLKEGDTDHV DSEGILENSI IGSKCEVNNG GNEGVTHVIT
     STELSPKNSN PVPDMSKFAA GITPFEFENM AESTGVYLRI RSVLKNSPRN QQKNKKASD
//
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