ID A0A158NJR0_ATTCE Unreviewed; 1374 AA.
AC A0A158NJR0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Calpain-D {ECO:0008006|Google:ProtNLM};
GN Name=105620899 {ECO:0000313|EnsemblMetazoa:XP_012057768.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012057768.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012057768.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; ADTU01018209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012057768.1; XM_012202378.1.
DR STRING; 12957.A0A158NJR0; -.
DR EnsemblMetazoa; XM_012202378.1; XP_012057768.1; LOC105620899.
DR GeneID; 105620899; -.
DR KEGG; acep:105620899; -.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; A0A158NJR0; -.
DR OMA; TQHCPQI; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 2.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF382; CALPAIN-15; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR Pfam; PF00641; zf-RanBP; 6.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00547; ZnF_RBZ; 7.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 6.
DR PROSITE; PS50199; ZF_RANBP2_2; 5.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 1..35
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 345..374
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 578..607
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 618..644
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 702..734
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 792..1097
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 37..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 857
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1021
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1041
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1374 AA; 152382 MW; 564B517B0C51E73B CRC64;
MGSIASVLQW HCSECALINP TESARCARCG LTRLRSDEKA SLDRRQDHAT SITAEHSGNA
SQGGGKETHA GDRAGRSTRR REDEECSARR ETSSGESTPP TPPPRADRLV ARNLTETLSV
DQSRSITVSQ GFERHLSAAD IRKNSHCCSL DGNSSDRKSL KRFSSLPSLA TQWTCIRCLL
DNNCSSLICA ACDANASIAQ NDGKQIGARK SKKINLHKEN RLKITSGLLA NVLDESVSKS
DSGNNVKINN TGMAQLTSIS RSDRGRGHHK DWILPSIGTM ESTTLPFTDN SDTSQRSPKR
HSPSMYERVK SKVSRSLSNG SVVQKLSEHM VQRPTSLVVP ETRQDDGLWS CDNCTLDNAP
GLEQCEACDA PRSPAPCSGV VISVPAWVPR ALSSAGPLSY RRSFSDADSV TNVTQKKTVN
RRSLNDEEPP AVPPHSIGFN SRPKYSYIGI TDPDIPPPLP KKQSSKLGLV PTKAHSEATS
PVGEVSNVSP LKRMWTCRKC SYAYNPLWSS GCDICGSSRS PPSLTQPSLI TVTKDTSNYP
THAQSPIVVS RDSVRYIPPK AATLATAESD LDDQIDPPSP VWTCKKCTLL NAASRTTCEA
CCGSKLKSIM HLEDATLRKG ESWVCPSCTL RNPLSTQNCN ACKTLADFLE VPKDNRAFGQ
RSPSPRLCST PTNSKAITPR HRNSVRRNGS SAAGDKRHSR TRDPSYIQWQ CKLCTYENKS
TTAICEMCQS SKSLSQASGD RGIPRLLESG TSTLRIQRQE SVVMENLRQL EERDALEKWE
RIVRYCKETN EPFVDDSFPP APKSLYYNPT DTKDNHVVQW RRPHQINVDS SVDSKLPWAV
FRTPLPSDIS QGVLGNCWLL SALAVLAESD ELVRRVLVMK ETCPEGAYQV RLCKDGKWTT
VLVDDLLPCD KRGHLVYSQA KRKQLWVPLI EKAVAKIHGC YEALVSGRAI EGLATLTGAP
CESVPLQPSA LPSEDELDRD LIWAQLLSSR QAMFLMGASC GGGNMKVDEE EYQRKGLRPR
HAYSVLDVRD VQGIRLLRLR NPWGHYSWKG DWSDDSPIWT PQLREMLMPH GASDGVFWIS
FDDVLKYFDC IDICKTRVGW SEVRLRGTLP PLSSLRHLSC VLLTVLEPTE TEFTLFQEGQ
RNSEKSQRSQ LDLCVVVFRT RSPAAPEVGR LVEHSKRQVR GFVGCHKMLE RDLYIVVCLA
FNHWHTGMED TSSYPEYVLA IHSSKRLLVE QISPPAFVLA DAIISLTLAK GQRHEGREGM
TAYYLTKGWA GLVVMVENRH VNKWIHVKCD CHESYNVVST RGQLRTADSV PPLHRQVIIV
LTQLEGSGGF SIAHRLTHRL ANSGNLHDWG PPDTQHCPQI DTQVEGLHSP RLIT
//
