ID A0A1S3F3S9_DIPOR Unreviewed; 795 AA.
AC A0A1S3F3S9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=2-5A-dependent ribonuclease isoform X1 {ECO:0000313|RefSeq:XP_012870865.1};
GN Name=Rnasel {ECO:0000313|RefSeq:XP_012870865.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012870865.1};
RN [1] {ECO:0000313|RefSeq:XP_012870865.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012870865.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_012870865.1; XM_013015411.1.
DR AlphaFoldDB; A0A1S3F3S9; -.
DR GeneID; 105985004; -.
DR KEGG; dord:105985004; -.
DR CTD; 6041; -.
DR InParanoid; A0A1S3F3S9; -.
DR OrthoDB; 2994922at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd10423; RNase_RNase-L; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.20.1440.180; KEN domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR042745; RNase-L_RNase.
DR PANTHER; PTHR24141; 2-5A-DEPENDENT RIBONUCLEASE; 1.
DR PANTHER; PTHR24141:SF1; 2-5A-DEPENDENT RIBONUCLEASE; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00580; PUG; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 6.
DR PROSITE; PS50088; ANK_REPEAT; 7.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT REPEAT 118..150
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 151..183
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 184..216
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 227..260
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 261..296
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 297..322
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 331..363
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 424..645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 648..782
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 89827 MW; 6FCD1ACAD8681B23 CRC64;
MPRFPSGLPS NRAHGSSSDR EPHWAPRGHV PLTVIQPQSI NVFTFSRGKQ KRSRRLSPPA
LTIMETQGAQ QEASKPSSRS DSMAEPRLWV IQAVREEDVD GLRRLLEGGA DANESDEWGW
TPLHNAAECG RQDLVELLLR YGAEPARRKR NGATPFIVAG IGGHVHLLRL FLSRGADVNE
RDSNGFTAFM EAAWHGRVEA LRFLFAQGAD VNASRETQED RRPLRGGGAT ALMDAAERGH
VEVVRILLEE MGADVNARDN MGRSALIHAL LDGGEQAEAV AGLLLDHGAD VRVRGEQGKT
PLILAVEKRR LALVRMLLEQ DALEIDDTDH EGTTALRAAV ELGSREMVRA LCDRGASVSC
GDLMRIARRH YDQALVKLLR EYGAQEHVHP PAEDWEPQSS HWGRALKSLH RIYRQPIGKL
KIFMVEEYKI ADTSKGGIYL GFYEGREAAV KLFPEGSPEA RQEMACLRSC RESSHFVTLY
GSESHRGCVY VCMALCEQTL EERLQGRPEE GLQSREDALA PNTLLSIFEA VRDLHVSHGY
THQDLQPRNF LIDSKDAVRL ADFDQSIKGT GDPQEIRRDL EALGRLVLYV VKKGEIPFET
LKGKNNEEVV QLSPDKETED LIRHLFYPGE NMTDCVGDLL GHPFFWTWEN RYRTLRNVGN
ISDIKTRKCT SEIYRLLHSD PSVSYSFDKW TSKIDKHVME KMNKFYAKKN GNVYQDIVGD
LLKCIRNLGE HIDEEQNRKI KETIGDPFCY FQKKFPDLVI YVYNKLKNTE YRKHFPQTNK
PAQPQCVRGV RVGEP
//
