ID A0A2D0Q696_ICTPU Unreviewed; 823 AA.
AC A0A2D0Q696;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ARL14 effector protein {ECO:0000313|RefSeq:XP_017314223.1};
GN Name=arl14ep {ECO:0000313|RefSeq:XP_017314223.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017314223.1};
RN [1] {ECO:0000313|RefSeq:XP_017314223.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017314223.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_017314223.1; XM_017458734.3.
DR AlphaFoldDB; A0A2D0Q696; -.
DR STRING; 7998.ENSIPUP00000027013; -.
DR GeneID; 108259338; -.
DR KEGG; ipu:108259338; -.
DR CTD; 120534; -.
DR OrthoDB; 75559at2759; -.
DR Proteomes; UP000221080; Chromosome 27.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR InterPro; IPR029264; ARF7EP_C.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR006612; THAP_Znf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR46481:SF4; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN 39; 1.
DR PANTHER; PTHR46481; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF14949; ARF7EP_C; 1.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF05485; THAP; 1.
DR Pfam; PF02892; zf-BED; 1.
DR SMART; SM00692; DM3; 1.
DR SMART; SM00980; THAP; 1.
DR SMART; SM00614; ZnF_BED; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF140996; Hermes dimerisation domain; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50808; ZF_BED; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00309}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00309}.
FT DOMAIN 1..57
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT DOMAIN 591..672
FT /note="THAP-type"
FT /evidence="ECO:0000259|PROSITE:PS50950"
FT REGION 469..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 92271 MW; F6109EDCBB733EF3 CRC64;
MSAVWKHFKV SEKDGRMAVC RQCSAELSRG GTSGKTYSTT SLIYHLKSRH PEQYAEYEKD
TGAAAAAKRK VPPSTPTPSV ADFLEKAKKF ANDSAKTKGI TKKIMEFIAL DDQAFSVVED
VGFRRLIDYI EPRYIMPSRR YFTDVCLPEM YNVISTHVHE LLATDIAALS FTTDIWSSDV
SPTSVLSLTA QWIDTDFKLQ KVVLHSQELR GSHTATAISE AFANMFDTWR IDRSKVHVVV
SDNARNMAEA MGDSDLKGIQ CMAHTIQLAV NEGVMSQRSI ADVIAIGRKI VGHFNHSPLA
YARLQSIQEQ FALPTKRLQQ DVSTRWNSTY YMLESLFAQK RILAAYTADY DLPATFTAHQ
WVVIENVLSL LAPFEQLTKE ISSSEASVAD VIPFLAALKR LLNKEAEKDN GVKTTKSTLL
EAVHTRFIQA ASEPLYCIAT VLDPRYKEHY LDVGTKQHTR EIIQAELDSG KPLGDGQGMH
CAGDGGDSAE RKRSRTDEPR TASLSDMFDE ILRENNPNAR QRTSSTTQQL DGYLSEVPIP
RSNNPLEYWR TNQGRFPDLA QMARRYLSAP CTSTDSERLF SAASHIIDEK RTRLECGKAE
KLLFIKKNLP LFLNKFPISK PQLAEQWVRS LGRKNFVPTT NSCLCSDHFL PDCFRDYNGK
QFLREDAVPT IFSHSAKEGA DGTKIELRKN RGGLGTKEES RSGSISDGGK QQFPKERRQT
TRDTGQKGKS GNDAYKRRGG AKVSSSDRQV MTAKSKVYDS RGLLISCGRD LCDCLDVDCM
GCFYPCPECS SRKCGVECRC DRKWLYEQVE VEGGEIIRNK FAS
//