SEPH_EMENI
ID SEPH_EMENI Reviewed; 1346 AA.
AC Q5B4Z3; C8V8V8; Q9UVC9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cytokinesis protein sepH {ECO:0000250|UniProtKB:P78621};
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase sepH {ECO:0000303|PubMed:11679062};
GN Name=sepH {ECO:0000312|EMBL:AAF15541.1}; ORFNames=AN4385;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF15541.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11679062; DOI=10.1046/j.1365-2958.2001.02605.x;
RA Bruno K.S., Morrell J.L., Hamer J.E., Staiger C.J.;
RT "SEPH, a Cdc7p orthologue from Aspergillus nidulans, functions upstream of
RT actin ring formation during cytokinesis.";
RL Mol. Microbiol. 42:3-12(2001).
RN [2] {ECO:0000312|EMBL:EAA60302.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CBF77635.1}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Required for early events during cytokinesis including
CC localization of cytoskeletal components to the cytokinetic ring.
CC {ECO:0000269|PubMed:11679062}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF15541.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CBF77635.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA60302.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF011756; AAF15541.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000076; EAA60302.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001303; CBF77635.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_661989.1; XM_656897.1.
DR AlphaFoldDB; Q5B4Z3; -.
DR SMR; Q5B4Z3; -.
DR STRING; 162425.CADANIAP00006073; -.
DR PRIDE; Q5B4Z3; -.
DR EnsemblFungi; EAA60302; EAA60302; AN4385.2.
DR GeneID; 2872180; -.
DR KEGG; ani:AN4385.2; -.
DR VEuPathDB; FungiDB:AN4385; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_001872_1_1_1; -.
DR InParanoid; Q5B4Z3; -.
DR OrthoDB; 1290401at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:AspGD.
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; IBA:GO_Central.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:AspGD.
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; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1346
FT /note="Cytokinesis protein sepH"
FT /id="PRO_0000396519"
FT DOMAIN 60..310
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 66..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1346 AA; 149793 MW; 7532849BB9E4D22D CRC64;
MVSRSNEGPE APHPASRTPG APAKGRLTRL GSSPSKRDDK AKDDRMGKTS AKDVAELKDY
QLGDCLGRGA FGSVYRALNW NTGETVAVKQ IKLADLPKSE LRVIMLEIDL LKNLDHPNIV
KYQGFVKSAE TLNIILEYCE NGSLHSIAKN FGRFPETLVG VYMSQVLHGL LYLHDQGVIH
RDIKGANILT TKEGLVKLAD FGVASRTTGL SESSVVGTPY WMAPEVIELS GATTASDIWS
LGCTVIELLE GKPPYYNLQP MPALFRIVND DHPPLPQGAS PAVKDFLMQC FQKDPNLRVS
ARKLLKHPWI VNARRSDSVV PKKSTEYEEA VKSVQEWNEA LRSPESNALR RGTRNENQNP
PSLRLDTRHT PTKVTLPSPV SRIVADKFSS PSSGEEDNWD DDFATAISPS ALQLPHLRPH
DNFGGMLSSE KLKAFASLDG TVLKSDESFE ESDDPFKGSL LAGEHDPLKT IRPPPSQQAN
SGTSQSQNGP YGAHMRRGPP LNTAITPVYG GQMLQNSSSP IRQQRPPLFY KENSVEDYSD
LISANEDVLD RKISAFQESD EHKDLADTGR SREVIRYQSS YEQEDTPRIG RQISVKRYRG
TVEIQQFAEN EHDEDFSDIL GVDGVTLDKA ESDDGSNKST LMLNTKLSNN SWLGDLDDED
DPFALLEEGL DETDLEANIA RDKHARLRSQ VEGLVGSLKT SQDEEVLGDI SEQLLAVFCD
FPETKNIIIS AHGMLPILEI LDLCRRRDIT LCLLKIVNAI IYDDYEIQEN LCFVGGIPII
NEFAAKKYPR EIRLEAAAFV QQMYQTSTLT LQMFVSAGGL NVLVEFLEDD YEDERDLVLV
GVNGIWSVFE LQGSTPKNDF CRILSRSSVL DPLSLVLSRV LDEEGELAEV VEGRIANIFF
IFSQAENHVK EMVSERTVLH RVLKELKRMT PAHQITMLKF IKNLSMLSTT LDSLQNSNAI
DVLTDLLRST IKRPHFREVS NQILNTIYNM CRLNKSRQED AALNGIVPLL QKIVKTERPL
KEFALPILCD MAHSGKVGRR ELWRNKGLAF YISLLSDPYW QVTALDAIFI WLQEETAKVE
EHLLENRYDQ PSFTDAIVRC LTLSKANAFE NILEPLQKLL RLSPPIASTL ARPDLFSRLG
QKLHHSKAAV RLNLLRIISS ICDSSEQQGG LLASYGLLDS IRELEHDPAI LVRDMAGKLI
QSSERNDSYG LCKLKPNVRR GSTSATSPGL LANQSAPVTP QLSRQNQSKG YYDSRETQRR
PRSAISGSAL ALRPGSRDGP TPGIVGGANG SAGASRNRIA RGVSNRLSHI ELLPNDDDRI
PSSITRRSSV LPRRRRLTQF EAERGS
