ID A0A068RPK9_9FUNG Unreviewed; 1745 AA.
AC A0A068RPK9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=LCOR_03480.1 {ECO:0000313|EMBL:CDH51934.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH51934.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH51934.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|RuleBase:RU004273};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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:CDH51934.1}.
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DR EMBL; CBTN010000011; CDH51934.1; -; Genomic_DNA.
DR STRING; 1263082.A0A068RPK9; -.
DR VEuPathDB; FungiDB:LCOR_03480.1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586}.
FT DOMAIN 448..483
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 733..805
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 904..1069
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1215..1376
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1583..1653
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 313..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1701..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1745
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1745 AA; 200235 MW; 92E02503D077EAC3 CRC64;
MTAVNSVDDV DAWIAQLSEC KQLPEADIKK LCDKAREVLL EESNVQPVRC PVTVCGDIHG
QFHDLQELFR IGGNSPDTNY LFMGDYVDRG YYSVETVTLL VALKLRYRDR VTILRGNHES
RQITQVYGFY DECLRKYGNA NVWKMFTDLF DYLPLTALIE DQIFCLHGGL SPSIDTLDQV
RALERFQEVP HEGPMCDLLW SDPDDRCGWG ISPRGAGYTF GQDIAETFNH NNGLTLVARA
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMEIDE HLKYSFLQFD PAPRKGEPHV
SRRTPDYFFL SNAMMPQQSP SGPTPPPSNT VPGNFNKDQF NGLLQRARVL QSQGFTEETN
AEFAQIMQML KSFQLQQKLQ QQRQNMVGGG GFQQSPMSPV QVPSQQPRPS QPRPPMPAQQ
QQQPQQPPPQ QQPMMDAPAS PAVPPHSVFT QAQLGALKYQ ILAYKLISKN MPLPQHIQQA
VLQPFPTTDD SSATTPLNMS VPVVGAGAER TTDPATSLTG AAAAAAVSNG IASPAGAGST
ATNSSKQPSV TASPQQTLQQ VVPQTTPSSS AQVPLPGQPA PDYNAYASPY NMLKKPITSY
AHASRQHRQL IPSITPVGVD SQKLSEERER RINEHIQDRI HELEKLSGSM IEKLKEQDIN
VKKSSASSTP LRSLIELKSL KLLDKQRKLR QEMTHGMSKA TQLATSADRI AFRRLKRQSL
REARVTERIE RQQRIDRENQ KKQKHMEQLQ IICDHGRNLI AAQRTWQAKQ NKLGRAVLQY
HQHVEKEEQK KAERISKERI RALRNDDEEA YMKLIDEAKD TRLTQLLKQT DAFLESLTKA
VVDQQNDPVH RHEYLAEEPG VEEDSSKVDY FKVTHRIKEE VSQPNILVGG TLKDYQIKGL
QWMVSLYNNH LNGILADEMG LGKTIQTISL ITYLIERKRQ NGPYLIVVPL STLTNWALEF
DKWAPSVAKV VYKGPPQVRR NLQMDIRRGD FQVLLTTFEY IIKDRPVLSK TKWLHMIVDE
GHRMKNTKSK LTLVLRQYYH ARYRLILTGT PLQNNLPELW ALLNFILPKI FKSVKTFEDW
FNTPFSNQGV QDKIDLNEEE QLLIIKRLHK VLRPFLLRRL KKDVEAELPD KVERVIKCKL
SALQLKLYQQ MKKNGRMYTS MSKEGKMGVK GLNNTIMQLR KICNHPFVYE EVENAINPSR
QSNELLYRVS GKFELLDRTL PKLRETGHRV LIFFQMTQVM SIMEDFMNYR GYRYLRLDGS
TKADDRSQLL QVFNSPDSPY FVFLLSTRAG GLGLNLQSAD TVIIFDSDWN PHQDLQAQDR
AHRIGQTKEV RIFRLVSANS IEENILARAN YKLDIDGKVI QAGKFDNRST DEDREAFLRS
LLEDKADEQN DVDGEEDIDD EELNEMLKRS DQELVIFNRI DADRDRAESE YYRRKGIRGR
IPDRLIQEDE LPEVYRHEET LVDDISPLLE YGRGQRVKDS VRYDDGLTEE QWVNALEDEN
VDLEELISRK EARRRKGKEL QEDANYLKKR GRPKKAEPEK KRSRARKDEE LSGPDPLPPQ
MRQQMTQIFE TCYRAVEDAE DEDGRKRNVL FMDLVSKRDY PIYYTMIKNP IAMKMIKKRI
HSPYYKSIQQ FRADFHLMFD NARTFNEEGS LVYQDADEMQ RIFDMTFAQL CPNDMLPPLP
MMDNPMLDMY GGGNGSGMAA PFQAVPGTMP GSKLEAPKKQ KRGPMEDEDE DAEDEDDDYD
DDYNE
//
