ID A0A1S3IW27_LINUN Unreviewed; 1099 AA.
AC A0A1S3IW27;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Uncharacterized protein LOC106167829 {ECO:0000313|RefSeq:XP_013402166.1};
GN Name=LOC106167829 {ECO:0000313|RefSeq:XP_013402166.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013402166.1};
RN [1] {ECO:0000313|RefSeq:XP_013402166.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013402166.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000256|ARBA:ARBA00006672}.
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DR RefSeq; XP_013402166.1; XM_013546712.1.
DR AlphaFoldDB; A0A1S3IW27; -.
DR STRING; 7574.A0A1S3IW27; -.
DR EnsemblMetazoa; XM_013546712.1; XP_013402166.1; LOC106167829.
DR GeneID; 106167829; -.
DR KEGG; lak:106167829; -.
DR InParanoid; A0A1S3IW27; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043067; P:regulation of programmed cell death; IEA:UniProt.
DR CDD; cd00022; BIR; 3.
DR CDD; cd08521; C2A_SLP; 1.
DR CDD; cd16713; RING-HC_BIRC2_3_7; 1.
DR CDD; cd14321; UBA_IAPs; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR048875; BIRC2-3-like_UBA.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10044:SF139; DEATH-ASSOCIATED INHIBITOR OF APOPTOSIS 2; 1.
DR PANTHER; PTHR10044; INHIBITOR OF APOPTOSIS; 1.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF21290; BIRC2-3-like_UBA; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00239; C2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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; PS50004; C2; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 23..144
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 916..945
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1052..1087
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 186..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_013402166.1"
SQ SEQUENCE 1099 AA; 123031 MW; 32B1CB2215FAF8A8 CRC64;
RSQGSLSGPC SNAEEDSYSN IPVFGKILLS MEYDYRKGWL IIHIYLCQDL APADVKKNRS
DPYVKTYLLP DKSRGGKRKT KIKKNTLNPT FDESLHYIVT KNELGRFLWL SFWHSVTFGH
NMFLAEVLLP LNKQNFADTS PQWFQLSGDH MAAGDRDQAI SNVTQPHSIK TTRGQVLNQA
HMGIQLQRSN SSKTSLQPNF ENQEDDFQSQ AAKKIVVQGQ FQQNQPSLLP KCGNQRLQRG
QFQSQTLPGE SAGPNQLCHQ EGQSQKSRLP QGPLTDHHLE EQVGVHFQTR RKSSHFFPPL
PQQQDSVGAG GQDQGVTDSQ TIRTMGNQVL NQADGDIHTH VSDLTLLSKK STQENTVTTD
PETDHHTNTS SVQNEVVAFF NRDKVQQREE KQYKCTKGNE GENDDHNIYR QVSVFLHRDL
LRYLTSYAPG RTCIHVYPLH LQEYFLRSAQ GPPFRVGEEY CYEAVRLSSF KDLPNSVPVP
ATRLAQSGFH YTGNSDEVVC FSCGGRLKEW TYGDNPFVRH RNFFPDCPLM NGTEVENVPL
FPRDPDSNFN IGANVDPFPN LANTRSTPRD QSGNWSSLLS SQQALSRPLG ITSPEVATLQ
FTPLESPLFP ANINGNTSVP SNASHRTSNV PSRMRNESDR LTTFVNWPSG AGVLPRDLAR
AGFFYVGMGD RVQCAFCEGV LRNWEPGDQP MQEHRRYLST CPFILGLEVG NIPVEEPSTA
LPLAVSESQR QAVGGSTTGS ENATNGATLG ILTARPRHEK YAIENTRVQT FANWPPSRIP
CPEELARAGF FYAGFGDNVK CFFCDGGLRN WEPQDDPWTE HARWFPRCGF VRQCKGDEFI
RMIKEQNSPN NQVSIYLVTS LRFTNGLGLT LYIGYTLHID LILFYSIYPS QAQTQTQRPQ
GAPGSYHVEA REIKARLDTP TVQAVLDMGF SRDTVRQAIE QRLRNTGDDF PSAATLFDAV
LNIEDENNRQ GAAAISVIPQ EEPGQQPLNA TLSEAPPHKA AQKTSQTQNT DKLSKKDKKK
KKQDAPVVKD SDDKETKSLI EENKRLKEER TCKICMDEEV SVVFLPCGHL VACVQCAPAL
RNCAICRAAI KGTVRSILS
//
