ID A0A498NC59_LABRO Unreviewed; 1116 AA.
AC A0A498NC59;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Ankycorbin-like protein {ECO:0000313|EMBL:RXN26955.1};
GN ORFNames=ROHU_020408 {ECO:0000313|EMBL:RXN26955.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN26955.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN26955.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN26955.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN26955.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN26955.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QBIY01012082; RXN26955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498NC59; -.
DR STRING; 84645.A0A498NC59; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24129; ANKYCORBIN; 1.
DR PANTHER; PTHR24129:SF0; ANKYCORBIN; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498NC59};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 28..349
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REPEAT 268..300
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 326..358
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 359..391
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 417..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 462..496
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 611..645
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 677..1092
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 417..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 125075 MW; CC0350C7662D2684 CRC64;
MDFCQYLIVY YFLAFTFFKV AVCSEVSIIG GKDVKKPLPW MVSIQKDEAH VCGGILIHNQ
WVLTAAFCKI TPTSSVTVLI GSLSLSKVSK GAQRVGIHSY KYPKTFNAET KQDDIMLIKL
NKKVKGKPQK IPKKEKDVPL GTNCVVTGWG TTNVKDSKPS DKLQMLEVMV MLRKRCNLYY
NGHPVITEDM LCAGGKQEKT GTCWVSWDLL ESEWTNMKSL KAKFRKSDAH EWNKNDERLL
SAVEHGEADK VTSLLSKKGA CPTKLDSEGK SALHVAATRG QAECLAVILA HGADVSLQDA
SAASGDTVIV QLLCEHKCHV NLKDSDGFTP LLLSARHAHT EVCQSLLDWG ADINARDKNG
RTAVLLASES SCPAAVELLV QRGADLQMVD SLGHDVLHYA KLSGSSEVQT ILNTALHRQQ
SESDKTSART PQSAGVFSPP YFTPTETPLS SKSDSSKRFN YKEEEELKSA VLKEEIEKLH
EEKSMLLETI EDLKQIVEQT EPKASTAQPF NIPSCGSCFD LQPLLLSGTH FNSCIFTGPG
QKRPAPQGEE GQGSSRPNSI ESNASYHSTR ADFELSSDVH IQTGDEEDLS ELSVLDISGS
PIKHEIEDDT RPSADKEIRL LRDALENLQT KLLESKMENR TLQARLNTDF EKIEVASKSM
GEDTQKCQEE LQEDNVVQKF QYLKSCLEQE VKDLKEKLAI SQEEQKQDSC LIKDLQAQLK
MVRLSEEERQ ELKNTYDTLV EDVNQEKALL IEKYKESQEE IRMLQEALRG TVPVEAAAKD
FEEMKAELGE IIDGLQRRLL ELSKSYSEAK SELSAARNQL QSKASEPKDK ADVACVTKEE
HEQKIQELVF KMKDMQKVLK DTEAKHQAAL KEIAQVKQDA ENQAQSSVAI ADHTQVVASL
GNAMKNLESE VEVLKEQLAQ KTSQVDALQS RLTVKKDVTP NDSLSRLEYE QMRKTLEGEI
SHLNHLLKDA LRKQDELALE VTTAWQEVKD ARNEREAAQE LAVSREQECS ALNTKYREAQ
EVIVQLKKQV ENHVISERDK NKKIDELSKE VMKLKEALNS LSQLSYTTST PKRQQNQQVD
SLQQQIKQLQ YQLAGLFSGL YVGEQEEVKR FPTEVF
//
