ID A0A1U7R5G8_ALLSI Unreviewed; 1127 AA.
AC A0A1U7R5G8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LATS2 {ECO:0000313|RefSeq:XP_006017685.1,
GN ECO:0000313|RefSeq:XP_025052413.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|RefSeq:XP_006017685.1};
RN [1] {ECO:0000313|RefSeq:XP_006017685.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-2022) to UniProtKB.
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 RefSeq; XP_006017684.1; XM_006017622.2.
DR RefSeq; XP_006017685.1; XM_006017623.3.
DR RefSeq; XP_006017686.1; XM_006017624.2.
DR RefSeq; XP_006017687.1; XM_006017625.2.
DR RefSeq; XP_025052413.1; XM_025196628.1.
DR STRING; 38654.A0A1U7R5G8; -.
DR GeneID; 102383095; -.
DR KEGG; asn:102383095; -.
DR CTD; 26524; -.
DR eggNOG; KOG0608; Eukaryota.
DR OrthoDB; 5348633at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21777; MobB_LATS2; 1.
DR CDD; cd05626; STKc_LATS2; 1.
DR CDD; cd14398; UBA_LATS2; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF149; SERINE_THREONINE-PROTEIN KINASE LATS2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_006017685.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 97..138
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 707..1012
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1013..1091
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 24..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 736
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1127 AA; 126643 MW; 4E1E12CF2B37C714 CRC64;
MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSGQVLPVG PGSETSLDPK ILVRKDAARQ
QQMRQTAKFG PYQKALREIR YSLLPFANES GTSATIEVNR QMLQELVNAG CDQEMAVRAL
KQTGSRSIEA ALEYISKMGY LDPRNEQIVR VIKQTSPGKG MVPNNVTRRP SFEGSNESFP
SYHQIGNATY EGTSFGAEGA DMLSDVPRPY MDYLISASQS AALNSPVQRP SAVGSHSAPG
SHQHQQKTYS ANIDSSVINY PGANHGSQAL QLQVTHGPNS PHYSRQHMMV QGEPMGYGIQ
RTPSFQNKMQ QEGGYANLPN KGTVVQNNSG HAFQQAPASL YIPHSHHKQT SPSSHQMHVI
ARGSAFANDF SDSPPQSLLT PSRNSLNMDL YDMNNPQVQQ WQTATPSRRD SLQSPGIETS
PRQHVTFRPD ATVPSRTNSF NNHQQQPQVP VSMRQVPPGK PDASITSPNT ITAVTSAHIL
QPVKSMRVMR PEPQTAVGPS HPGWLPAQTP AVDGLEIIEP HQLPVGGANA YQLEVDYSSQ
EPRCPPPPYP KHLLLPSSSE QFDINCLCMG VEQTLRGVPT STCSKAEENG ERNDKSSKNA
KMEKPGKDKK QIQTSPVPVR KNGKDEEKRE SRIKSYSPFA FKFYMEQHVE NVIKTYQQKI
NRRLQLEQEM AKAGLCETEQ EQMRKILYQK ESNYNRLKRA KMDKSMFVKI KTLGIGAFGE
VCLACKVDTH ALYAMKTLRK KDVLNRNQVA HVKAERDILA EADNEWVVKL YYSFQDKESL
YFVMDYIPGG DMMSLLIRME VFPEHLAKFY IAELTLAIES VHRMGFIHRD IKPDNILIDL
DGHIKLTDFG LCTGFRWTHN SKYYQKGSHI RQDSMEPSDL WDDVSNCRCG DRLKTLEQRV
KKQHQRCLAH SLVGTPNYIA PEVLLRKGYT QLCDWWSVGV ILFEMLVGQP PFLAPTPTET
QLKVINWEST LHIPSQIKLS PEASDLITKL CCAAEDRLGR NGADDIKAHP FFNSIDFSTD
IRRQPAPYVP KISHPMDTSN FDPVEEESPW NDASGDSTRT WDPLASSNSK HTEHAFYEFT
FRRFFDDNGY PFRYPKPSGI EVSQSEKCDV ENKDVVDQTG ACQPVYV
//
