SEPH_ASPTN
ID SEPH_ASPTN Reviewed; 1342 AA.
AC Q0CL79;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 79.
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:0000250|UniProtKB:P78621};
GN Name=sepH {ECO:0000250|UniProtKB:Q5B4Z3}; ORFNames=ATEG_05555;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1] {ECO:0000312|EMBL:EAU34624.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU34624.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476600; EAU34624.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001214733.1; XM_001214733.1.
DR AlphaFoldDB; Q0CL79; -.
DR SMR; Q0CL79; -.
DR STRING; 341663.Q0CL79; -.
DR PRIDE; Q0CL79; -.
DR GeneID; 4320592; -.
DR eggNOG; KOG0198; Eukaryota.
DR OrthoDB; 1290401at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; -; 2.
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..1342
FT /note="Cytokinesis protein sepH"
FT /id="PRO_0000396518"
FT DOMAIN 61..308
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 658..695
FT /evidence="ECO:0000255"
FT COMPBIAS 32..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 67..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1342 AA; 149981 MW; 869020ACCA1C5BB3 CRC64;
MVSRSSEGAE GPPPSAPKPP NTPAKSRLSR LGSSPSKRED KSRDDRMIKS SAKDVAELKD
YQLGDCLGKG AFGSVYRALN WNTGETVAVK QIKLADLPKS ELRLEIDLLK NLDHPNIVKY
QGFVKSAETL NIILEYCENG SLHSIAKNFG RFPENLVGLY MSQVLHGLLY LHEQGVIHRD
IKGANILTTK EGLVKLADFG VASRTTGLSE SSVVGTPYWM APEVIELSGA TTASDIWSLG
CTVIELLEGK PPYYNMQPMP ALFRIVNDDH PPLPQGASPA VKDFLMQCFQ KDPNLRVSAR
KLLKHPWIVN ARRSDSVVPK SSTEYEEAVR SVQEWNEALR SPSAGTLRRP VKHDQSPIPV
PPTRHTPTKD TLPSPVSRNV TDRFRSPVPT EEEEDNWDDD FATAISPSAL QLPHLRPHDN
FGGMLSSEKL KAFASLDGTM IKSDDSFGDS DSSFGSSRRS DEPDPLETIR PYPLKQPTAE
STQLQELPRS QINKTSMASM HHVPILTQNP TPPTKQPRPA SYYKENSIED YSDLIQANED
VLDSKLGAFQ EADENVDPFE SSPSKEAIRN RASAEDVMGQ QPQLRKQISV KRHRSAVEIQ
RFAENERDED FSDLLGTDEV MIDQPESDGS SDQSTLMLNS KLSNNSWLGD QDDEDDPFAQ
LEEGLDEMDL EANIARDKHA RLRNQVEGLV SSLKTSQDED VLAEISEQLL TVFCDFPETK
NIIISAHGML PILEILDMCR RRDITSCLLK IVNAIIYNDY EIQENLCFVG GIPIINEFAS
KKYPREIRLE AAAFVQQMYQ TSTLTLQMFV SAGGLNVLVE FLEDDYEDER DLVLIGVNGI
WSVFELQGST PKNDFCRILS RNSVLDPLSL VLSRVLDEDG ELAEIVEGRI ANIFFIFSQA
ENHVKEMVAE RTVLHRVLKE LRRMTPAHQI TMLKFIKNLS MLSTTLDSLQ NSNAIDVLTD
LLRATMKRPH FREVSNQILN TIYNMCRLNK SRQEDAALNG IVPLLQKIVK TERPLKEFAL
PILCDMAHSG KVGRRELWRN KGLAFYISLL SDPYWQVTAL DAIFTWLQEE TAKVEEHLLD
HRPDRPSFTD SIVRCLTISK ANAFENLLEP LQKLLRLSPP IASTLARPDL FTRIGQKLHH
SKAAVRLNLL RIISSICDSS EEQGGLLAKY GLLDAIRELE HDPAILVRDM AGKLIQSNEK
SEAYGMGKRK PMVRRRSTSA TPPNLLANQS APSTPQMNRT SQSKAYYEGK EGSRHPRNAL
SGSALALRPG SRDGSTPSLT AGLNGSTGAS RTRLPRGVSN RMSHVDLLSE EDSARPSSSL
SRRQSVLHRR RRQTQADADW TP
