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Database: UniProt
Entry: A0A452HGF1_9SAUR
LinkDB: A0A452HGF1_9SAUR
Original site: A0A452HGF1_9SAUR 
ID   A0A452HGF1_9SAUR        Unreviewed;       700 AA.
AC   A0A452HGF1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000013940.1};
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:ENSGAGP00000013940.1, 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:ENSGAGP00000013940.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A452HGF1; -.
DR   STRING; 38772.ENSGAGP00000013940; -.
DR   Ensembl; ENSGAGT00000015960.1; ENSGAGP00000013940.1; ENSGAGG00000010623.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006301; P:postreplication repair; IEA:UniProt.
DR   CDD; cd01702; PolY_Pol_eta; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.1170.60; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR041298; UBZ3.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR45873; DNA POLYMERASE ETA; 1.
DR   PANTHER; PTHR45873:SF1; DNA POLYMERASE ETA; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF21704; POLH-Rev1_HhH; 1.
DR   Pfam; PF18439; zf_UBZ; 1.
DR   PIRSF; PIRSF036603; DPol_eta; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR   PROSITE; PS50173; UMUC; 1.
DR   PROSITE; PS51907; ZF_UBZ3; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          9..262
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   DOMAIN          614..648
FT                   /note="UBZ3-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51907"
FT   REGION          533..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  76194 MW;  F4134A02ACD2B93B CRC64;
     MSRGRERVVA LADMDCFFAQ VEQRREPRLR GQPCAVVQYD AWRGGGIIAV SYEARAFGIS
     RGMRADEAQK RCPQLVLARV PEAYGKADLS RYREASVEVM KVMSRFAVIE RASIDEAYMD
     LTGAVQERLK KMQGQPIPAE LLPTTYIQGL PNVSTTAAKK KSVDCKEDLR QRGLHQWLES
     LPFGDISCPE LQLTVGAVIV EEMRAAVEAV TGLRCSAGIS HNKALAKLAC GLNKPNRQTL
     VSQGSVPQLF SHMPISSIRN LGGKLGASIT DVLGVEYMGQ LTLFSESQLQ THFGDKTGSW
     LYDMCRGIEQ EPVKPRQLPK SIGCSKNFPG KVALTTQKQV QHWLLQMALE LEERLSKDRD
     QNCRVAKQLT VSIRMQGDQR ASALSRCCAL PRYDAHKISS DAFMIIRNCN VAGAQQAAWS
     PPLTFLHIYA SKFSEAPTLS PAGIAAFLTS DAQCTLPAGT NATSPNAKCI GSPRKEPSKK
     PMNAIESFFR KAAERQRAHG AREPCLPAVP SAEAELSVPD PCGHNEREGL VLSKSQTPEA
     LVRHSPKGGS SPSPYRWLPP EELLPYPAET PSAGPASRST VKTESAGAAA SELPAWKEQS
     LPPSAGFVQG PASSPADQLH CEKCGQQVPV WELLEHMDYH FAVELQSSFL EASPLRAPAA
     APSSPAKSKS NAKTSGGSSA KRPRQGVTRT LEFFFKRLPP
//
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