ID A0A452ITF7_9SAUR Unreviewed; 1466 AA.
AC A0A452ITF7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=RanBP2-type domain-containing protein {ECO:0000259|PROSITE:PS50199};
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:ENSGAGP00000031161.1, 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:ENSGAGP00000031161.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 38772.ENSGAGP00000031161; -.
DR Ensembl; ENSGAGT00000035335.1; ENSGAGP00000031161.1; ENSGAGG00000022386.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 4.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR013913; Nup153_N.
DR InterPro; IPR018892; Retro-transposon_transp_CS.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23193; NUCLEAR PORE COMPLEX PROTEIN NUP; 1.
DR PANTHER; PTHR23193:SF23; NUCLEAR PORE COMPLEX PROTEIN NUP153; 1.
DR Pfam; PF08604; Nup153; 1.
DR Pfam; PF10599; Nup_retrotrp_bd; 1.
DR Pfam; PF00641; zf-RanBP; 4.
DR SMART; SM00547; ZnF_RBZ; 4.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 4.
DR PROSITE; PS01358; ZF_RANBP2_1; 4.
DR PROSITE; PS50199; ZF_RANBP2_2; 4.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 653..682
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 718..747
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 788..817
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 846..875
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 153084 MW; 069CAEF4DB1E2069 CRC64;
MASGGGGGGS GGGKIRTRRY HLGASKPYPR NKQQGIISRV TESVKNIVPG WLQRYFNKSE
DECVDASEPT SQQETPVNYH HGYADDDTPV FDGMVTPEST RINLEEPSTS RSALNFSDVL
TRPSLHRSHL NCTMLDSPSP HCQPSTSSAF AIGSSGLSLV KEIKDSTSQH DDDNISTTSG
FSSRASDKDI AVSKNTSVPP LWSTETERSH SLTQHSATSS KKPAFNLSAF GALSPSLGNA
SVLKTSQLGD SPFYPGKTTY GGAAAAARQS KIRITPYQTP VRRQMKAKQA NVQSYGVTSS
TARRILQSLE KMSSPLADAK RIPSSVASPL SSPVDRNMLD ITRFHLKRKQ VESQHPPVQK
LVTPKTISQS MSRLQYFKPS LTPAAESGKI RQRVDVKHKG VREKNLTAEQ QVEPTESNFT
YPKFSTPASN GLYSGVGGGG GGKMRKERGV HYVSQPGQEK QEVEAPVLPK IPLPINTASL
PNFSFGSLAS TTTVSSSPIT NTQPVINKMQ PASNASSPVF RFSSPIVKST EAEVLPPLSI
GFTFSVPVVK STQASGSSDT PVPLLISPGT TAVNSTSNKK KEKEEYDGAF KPAKVLKEGS
VLDLLKSPDF TSLKTHTPTA TQPVSTSTEV YTRPAISNFS AGSLGFRETS KQASSYWRCD
TCLLQNKATD NKCIACQAAK VPTADPAKQT GTLTLSSTVK STAPATGTLG FGDKFKLAAG
TWDCDTCLVQ NKPEATKCVA CETPKPGTGV KPALTLPVVT ENTITVTSSP SCTETTVTLG
FGDKFKKPKG SWDCTVCLVS NKAEDSKCIA CQCERPGGSV PVTSSSTSSF SAPSGGFLGL
DKFKKPEGSW DCETCLVQNK AEATKCIACE NAKPGTKPEL KGFGTAAVSS DAAAPSFKFG
IQSSSSESSQ TLGSTESFKF GEQGGLKFGI TSESGSVTNN MTGGFSFSKT SEDFKFGVSS
SDSKSEESKK DSKNNSFNFG LPSGTSNPST SAFQFGTSSL GQQEKKEEPV LGGFSFGTSS
TASMATSENK TGVSGFSFGT VAEKEVAATP FLFKKSEEKK DETPSAKGGF TFGSMEPASA
SQFVLGRTEE KQDAVTSATS LMFRKTVDNE EPKAQPIFSF GKSEQTKEES TAKPSFSFNL
TKPEEKETEQ TKPTFTFGAQ TSTADQGAAK PAFGFLSSGS SSTAIPSTSA NSSIVFGSSS
SASNPPPVAA AFLFGQASNT VSSSAFGNAS ESNAPQSFGF SQENKPATTS SSTGAAVGSF
LFGSGTGSNN TATPGFNFGA TSTSTSTGSS SSFVFGSGSS APAAGASQTP AFGASQMPTF
GQSQGASQPN APTFGSLSST SLFSAGSQPA PAAFGSVSSS SQPPVFGQQA SQQPGFGSST
APNSGAVFQF GRSDTNFSFT SNSPGVFTFG GNPGAPAPPT QPSSSSGFPF NPTPAFTMGS
NGKNIFSASG SSVSGRKIKT AVRRRK
//