ID A0A1J1HRI3_9DIPT Unreviewed; 1186 AA.
AC A0A1J1HRI3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=CLUMA_CG004385, isoform A {ECO:0000313|EMBL:CRK90688.1};
GN ORFNames=CLUMA_CG004385 {ECO:0000313|EMBL:CRK90688.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK90688.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK90688.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Bcl-2 family.
CC {ECO:0000256|ARBA:ARBA00009458}.
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DR EMBL; CVRI01000020; CRK90688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HRI3; -.
DR STRING; 568069.A0A1J1HRI3; -.
DR OrthoDB; 4833506at2759; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd22718; FHA_SNIP1; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.437.10; Blc2-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24394:SF29; GM08392P; 1.
DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00337; BCL; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF56854; Bcl-2 inhibitors of programmed cell death; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 88..115
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 351..378
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 379..406
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 407..434
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 435..462
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 463..490
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 491..513
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1071..1134
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 278..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 135047 MW; 0BBE54F2F733F28C CRC64;
MESKQEFPTF CYNMKNIQVL APTAQGGNTV NLAQIDDNNK TIQYIAQPFT TSYGQSYTLV
NPVQLAGQNG QIVINKPISS NTISNISFKC DVCSQIFSHL TLLNQHKRTH NQEDSHNDTV
TVVTQNQGLI QAQNLISESG QNLGQIQIVA TDSLEPAQLH HTLGDQINLV QQQPQHKGDK
NKCITCGSHI QQNAKRKGPK LIRCETCIQN DVNAQNVRPT QIFVSPDGDI KFEVNEMNQN
IIQLQGGVQK PPTKKKNVTT VTKCTTCNGT GVVIVTENPS SSSPVTSPQS TKISSARTIT
TTSPQKVQQV QIQHVKQHTT SPPPLQMHHQ VQHHAPPANQ GARQSENDKP FTCNICGGKF
SRYSSLWSHK KLHSGEKNYK CDQCSSSFAK AVYLKNHMRI HSGEKPYRCN TCGMTFSQSP
HLKNHERTHT GEKPYVCQIC DKGFARHATL WNHRRIHTGE KPYKCERCSS AFSQAAHLKN
HEKVHLGIKP YKCNICAGSF SDKFALKRHT NIHQKYGQTI PLHADVNEET LGDEAMLKEE
DEEDDSSMKD DMIMTAIFTP EVIFTSSDDL APPRTILKAT RTLVDRKFSF PASFHASKLL
ANDSNAFGRT SRRLSNVSDR VTDRVRKLST AIGWHQSPSK DILLSQGKYL ITLYIRFRLK
RAASLNQQKK KIGLQKMQRT LLIGADIKDV YIALKEAASV LEGLHAKIYT NVSRQLSNSP
KSLESAEDIA MLLTTFGKIL FKNDITWGKV ISLFSVTAGL SIDLVRQNQE DYIPTLIEGF
LGVIEDELIP FLSENNGWIS LHNRLQNKEK SVSTEWLYNY QISLKSMSKT KKKSKHQSDS
DSSSSSSSSS SDERHKKSKK QPTKDKDSKP EHSIWDSPRN QSSSSRRRNH SEERQKERKR
SHDQMERDSR QRNQRDDDRR NDSNRRRSPD RRDRDDNRRR SPDDRRRHED SRGYRKDHDR
DRRRRSRSRD EQRGGRFNRQ RRHNDKEDDD GNYEWGKRGI KKDPDEEPVE KDKPNFGLSG
KLAEDTNKVN GIVIKYAEPP EAKIPKRRWR LYPFKGETAL PTLYIHRQSA YLIGRDRKIC
DLAVDHPSCS KQHAALQYRL VPYERDDGSS GKRVRPYIID LESANGTFVN NKKIDSKKFV
ELLEKDVIKF GFSSREYVLL HEASKDEAED DNVAEEEEPP TVATAE
//
