SEPH_ASPNC
ID SEPH_ASPNC Reviewed; 1336 AA.
AC A2QHV0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cytokinesis protein sepH {ECO:0000250|UniProtKB:Q5B4Z3};
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase sepH {ECO:0000250|UniProtKB:Q5B4Z3};
GN Name=sepH {ECO:0000250|UniProtKB:Q5B4Z3}; ORFNames=An04g01130;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1] {ECO:0000312|EMBL:CAK38570.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Required for early events during cytokinesis including
CC localization of cytoskeletal components to the cytokinetic ring.
CC {ECO:0000250|UniProtKB:Q5B4Z3}.
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:0000250|UniProtKB:P41892};
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:0000250|UniProtKB:P41892};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P41892};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AM270068; CAK38570.1; -; Genomic_DNA.
DR RefSeq; XP_001401478.1; XM_001401441.1.
DR AlphaFoldDB; A2QHV0; -.
DR SMR; A2QHV0; -.
DR PaxDb; A2QHV0; -.
DR PRIDE; A2QHV0; -.
DR EnsemblFungi; CAK38570; CAK38570; An04g01130.
DR GeneID; 4990515; -.
DR KEGG; ang:ANI_1_1584184; -.
DR VEuPathDB; FungiDB:An04g01130; -.
DR HOGENOM; CLU_001872_1_1_1; -.
DR Proteomes; UP000006706; Chromosome 6L.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1336
FT /note="Cytokinesis protein sepH"
FT /id="PRO_0000396517"
FT DOMAIN 59..309
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 654..682
FT /evidence="ECO:0000255"
FT COMPBIAS 1211..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 65..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1336 AA; 149659 MW; 566E59230F6C57ED CRC64;
MVSRSSETSE GPPPPSKIPG TPAKTRLSRL NSSPAKQDKP KDDRVVKSSA KDVAELKDYQ
LGDCLGKGAF GSVYRALNWN TGETVAVKQI KLVDLPKSEL RVIMLEIDLL KNLDHPNIVK
YQGFVKSAET LNIILEYCEN GSLHSIAKNF GRFPENLVGL YMSQVLHGLL YLHEQGVIHR
DIKGANILTT KEGLVKLADF GVASRTTGLS ESSVVGTPYW MAPEVIELSG ATTASDIWSL
GCTVIELLEG KPPYYNLQPM PALFRIVNDD HPPLPQGASP AVKDFLMQCF QKDPNLRVSA
RKLLKHPWIV NARRSDSVVP KKSTEYEEAV KSVQEWNEAL RSPDTGTLRK PYRYDAQGAA
LRPEMAPSRY TPTKDILPSP VSKHVTDRFR SPDSTEEDNW DDDFATAISP SALQLPHLRP
QDNFGGMLSS EKLKAFASLD GTVLKSEDGF DDFDDPFSQQ PGESDPLRTI RPYSAKPTGM
ENMSQQTKPT IAAMHHNVPV LKTPVPPLRP QRPTSYFKEN SVEDYSDLIS ANEDILDDKL
SAFQDIDEEG SDISIPSPSK EVVRYQASPD HDEDHQPQLR KRISVKRHRS AIEIQKFAEN
ERDEDFSDIL GADEVALDKP ESDEGSDRST LMLNSKLSNN SWLGDQDDED DPFAQLEEGL
DEVDLEANIA RDKYARLRGQ VEGLVSSLKT SQDEDVLGEI SEQLLTVFCD LPETKNIIIS
AHGMLPILEI LDICRRRDII LCLLRIVNAI IFNDYEIQEN LCFVGGIPII NEFASKKYPR
EIRLEAAAFV QQMYQTSTLT LQMFVSAGGL NVLVEFLEDD YEDERDLVLI GVNGIWSVFD
LQGSTPKNDF CRILSRNSVL DPLSLVLSRV LDEEGELAEI VEGRIANIFF IFSQAENHVK
EMVAERTVLH RVLKELKRMT PAHQITMLKF IKNLSMLSTT LDSLQNSNAI DVLTDLLRST
IKRPHFREVS NQILNTIYNM CRLNKSRQED AALNGIVPLL QKIVKTERPL KEFALPILCD
MAHSGKVGRR ELWRNKGLAF YISLLSDPYW QVTALDAIFT WLQEETAKVE EHLLDNRYDK
MSFTDSIVRC LTISKANAFE NILEPLQKLL RLSPPIASTF ARPDLFTRLG QKLHHNKAAV
RLNLLRIISS ICDSSEEQGG LLAKYGLLEA IRELEHDPAI LVRDMAGKLI QSNERSESFS
LEKRKPGMRR KSTSTTPPGY LANQSAPATP QINRFNQPKA YFDGRESQRH PRPSLSSSAL
ALRPGSRDGT GPSLSAGLSS SAGPSRNRLS RGVANRLSQV ELLAEEETRP SSSLSRRRSI
LPQRRRPTHA DSDWAS
