ID A0A452HXD3_9SAUR Unreviewed; 611 AA.
AC A0A452HXD3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Baculoviral IAP repeat containing 2 {ECO:0008006|Google:ProtNLM};
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:ENSGAGP00000019795.1, 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:ENSGAGP00000019795.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000256|ARBA:ARBA00006672}.
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DR AlphaFoldDB; A0A452HXD3; -.
DR STRING; 38772.ENSGAGP00000019795; -.
DR Ensembl; ENSGAGT00000022557.1; ENSGAGP00000019795.1; ENSGAGG00000014596.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd00022; BIR; 3.
DR CDD; cd08329; CARD_BIRC2_BIRC3; 1.
DR CDD; cd16713; RING-HC_BIRC2_3_7; 1.
DR CDD; cd14394; UBA_BIRC2_3; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR048875; BIRC2-3-like_UBA.
DR InterPro; IPR041933; BIRC2/BIRC3_UBA.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR10044:SF79; BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR10044; INHIBITOR OF APOPTOSIS; 1.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF21290; BIRC2-3-like_UBA; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF57924; Inhibitor of apoptosis (IAP) repeat; 3.
DR PROSITE; PS01282; BIR_REPEAT_1; 2.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 446..536
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT DOMAIN 564..599
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 357..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 420..447
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 357..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 69220 MW; 7662881A69889CD9 CRC64;
MNIVESSSFL ANLMNNSTVC ELKYELSCEL YRMSTFSTFP LNVPVSERSL ARAGFYYTGV
KDKVKCFSCG LMLDNWKQGD CALEKHKQLY PSCSFVQNLL SVSNLGSSSH SAFSPPATIN
SFSPSLHSIT GAPSLEQIGF FSTTFSSFPQ EPVTSRAVED PSHLRSNFYN PAMSTEDARL
CTFQTWPLTF LSPTDLAKAG FYYTGPGDKV ACFTCGGQLS NWEPKDNAMS EHRRYFPNCP
FVENKARGHP IFSISNQSMQ THVARVKTFI NWPTRIPVRP EQLANAGFYY VGRNDDVKCF
CCDGGLRCWE SGDDPWIEHA KWFPRCEYLL RIKGREFVNQ IQARFPHLLE QLLSTSDTPV
DESANPPTIH SESRESHSED AIMMNTPVVK AALEMGFSRR LIKQTVQSKI LATEENYKTV
NDLVSDLLTA EDEKREEEKE RQSEEVASDD LSLIRKNRMA LFQHLTCVLP ILESLLSAKV
ITELERDVIK QKTQTPLQAR ELIDMILVKG NAAAHIFRNC LRECDPMLYK DLFVEKNMKY
VPTEDTLGLP MEEQLRRLQE ERTCKVCMDK EVSIVFIPCG HLVVCKECAP SLRKCPICRG
TIKGTVRTFL S
//