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Database: UniProt
Entry: A0A1X2HHI3_SYNRA
LinkDB: A0A1X2HHI3_SYNRA
Original site: A0A1X2HHI3_SYNRA 
ID   A0A1X2HHI3_SYNRA        Unreviewed;      1996 AA.
AC   A0A1X2HHI3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=BCR43DRAFT_454648 {ECO:0000313|EMBL:ORY98518.1};
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706 {ECO:0000313|EMBL:ORY98518.1, ECO:0000313|Proteomes:UP000242180};
RN   [1] {ECO:0000313|EMBL:ORY98518.1, ECO:0000313|Proteomes:UP000242180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORY98518.1,
RC   ECO:0000313|Proteomes:UP000242180};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000256|ARBA:ARBA00010769}.
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:ORY98518.1}.
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DR   EMBL; MCGN01000003; ORY98518.1; -; Genomic_DNA.
DR   STRING; 13706.A0A1X2HHI3; -.
DR   InParanoid; A0A1X2HHI3; -.
DR   OMA; AYERTIM; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000242180; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00892; PIKKc_ATR; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR012993; UME.
DR   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF72; SERINE-PROTEIN KINASE ATM; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF08064; UME; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242180};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1031..1564
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          1667..1984
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          1964..1996
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   1996 AA;  227595 MW;  0B81DD116319D463 CRC64;
     MDGLEGPYNE FVKADKILRE MVEEVLSKET DQDDNEAQVS PALDVLRSND DGSLLLNRLV
     SSFVHRVEER LYTIAKAETR PRRSVPSSRR RLHSLSPYRQ PSAMTSEKAA GVINLLLFFS
     GVVEKLPRNL GIFMDGTSLW QSLSLFSEGS LINYPNGCTA LSTALVALWE KFNRSSICRS
     SYQAEQYLCC ILRVMNALCA ASTFNHIPQL SDCVTKLFAP TQLRVTDQDT MLSLLESLSR
     HKSNDSTEYY IQAVVLKVAC ILMVHMVEIP WISTYLKDLS KILQLRVLAT EADVLLRQLE
     NAKSPDMDTS IAYESMDISQ ITTASDEQGT QQYPKEIIKV WNPLMDLIPG LLSVVDMEPS
     QANAALDQLQ ILSSELQLPP NLLLAGKEQA VTEILTRYLG INMQISDRLA GFYGLDIKSL
     LQSELQYAIP YAFRQSDDHL VMVMVSYLQT DTRTLVESGI VFILVDLLLS TNAAVSQTGF
     DKLKQVYQSE DAPAELLRSH RTKVSAQLAM HLAIPPLRAK AQNALEMVIK SCGDLVPTAL
     PEYMSTIVLA FLHEVDDYLY EKRRGRSGRA SANALKALNE VMGILGTRTK EHAPRFMALI
     STVGEIPGLH TDAFMLWDRL IQELHSDDLH NHFSPILVAL LDLYTLFDAR GRMRISDVIW
     DMIRRCDADK ITPYMLPVIP DFDDLKSLKL FVDEKQQALQ PEDIVVHFLA QAKSYDVAST
     LLALGHLKTV LENHGPLHEA VLQHQSSLIS TLLFLSRRNI EQRIHREAAI CLGMLGAVDP
     SRCNVKPLDE TLIIIDFGSD KETRRFILKL IVAQLIPAFH AANDTLIHQR LQYTMQTLLK
     LGGFSEHIAK RTQDGQDIRE AWKTLPVAAK ALLTPLLRSS YKATYSCIPQ ASPIYPTASN
     FQIWVQTWYF QLQAAMQGRT KAIFDACIPV VISGNTAVTV WLLPYMVSHV LFTGSPQDKK
     SIALEVESVL EINSRPDVVN ETLRQLSLQI VVSVTEYCRK WIRQVQRSAK GVLPTAVESY
     RSFLNTFPND KMAAASYLSQ AYAQALMHME MHIRSYKDHE DAIRKEDLDM LRQIYPHMDD
     SDSMEAIFEF YSQPLSVEET VSKLVSGDHW NDAKAFYEDM QQWDDPKEAV NGLFQCYSVL
     GDYVGMYAQA QLLRDNYAGL PKMRSRLNAY TQESLLHIGA WDRLERVLNE PSEDIFSVRL
     AKAMLHIRKG HYYDAFSQIN EARQDQSMDL ANFGTDSYRR CYKSVLRLQI LQDLEDYQIA
     FETAYKEDRL DLLNHLHIQW EKQFNLFAPS YEVRSMMLEL RHIVAFQMHD HGKGTSAWEA
     NSWLLRAKLA RKAGYMETAN DSLVKAERLG ATDVEVERAK WLWLKGKQEE AYKHLNTCRK
     LSAKGLLLRA RYFQRLPETN INRVYAHYRA ASKEGPTYEK IAFMLGRFLD NWLEQRSQSL
     GSKWRLPNII KVTEKMIESY SEALCLGSRY NLESMPRLLT VWFQLAQKPM EEGRQEAFVN
     GTKIIREKLP GMPAYQFLHV LPRVISWLSH ENAVVGDILM EIVHKVFTAY PRTTIWSLQA
     ASHSSKENMR SRANAIINRV KSSQDTAYIS KIIHDAEEFC SGIYELTYSR MDMQENSQRI
     DPRSKIGKLK DLSIAIPNQR AFIPTLPETV DQDYIPFADD IPTIRCIAPQ VTVMRSLQQP
     KKIVLQGSDG RQYPFLCKKN DDLRKDARMM DFCFMINKFL EKDPEARQRK LYIRTYAVLP
     LGENWGLLEW LNNLNPLKAI VSSLWQAMGI EPRAILLTAK QQLEKRPAEE QIVIFRKLVQ
     RCPSVFYRWF LEKFPEPSQW FVCRSRYVKT LAVMSIVGYI LGLGDRHAEN ILFDATTGDC
     VHVDVNMLFD KGKHLGVPEI VPFRLTRNLV GAMGPLGYEG LFTKSCQVTL DVLRLHRGQL
     LSVFETLVYD PISEWHSRQR INTEEQLQAT AKKELSKIQN KISSNKTVKQ EVASLIATAS
     DDTNLAQMFV GWAPFI
//
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