ID A0A094ER95_9PEZI Unreviewed; 2177 AA.
AC A0A094ER95;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Conserved oligomeric Golgi complex subunit 4 {ECO:0000256|ARBA:ARBA00020975};
DE AltName: Full=Component of oligomeric Golgi complex 4 {ECO:0000256|ARBA:ARBA00031340};
GN ORFNames=V500_11597 {ECO:0000313|EMBL:KFY81256.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY81256.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY81256.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the COG4 family.
CC {ECO:0000256|ARBA:ARBA00009215}.
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:KFY81256.1}.
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DR EMBL; JPKC01003668; KFY81256.1; -; Genomic_DNA.
DR STRING; 1420913.A0A094ER95; -.
DR HOGENOM; CLU_001049_1_0_1; -.
DR Proteomes; UP000029284; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1970; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR048682; COG4.
DR InterPro; IPR048684; COG4_C.
DR InterPro; IPR013167; COG4_M.
DR InterPro; IPR048680; COG4_N.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24016; CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 4; 1.
DR PANTHER; PTHR24016:SF0; CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 4; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF20662; COG4_C; 1.
DR Pfam; PF08318; COG4_m; 1.
DR Pfam; PF20663; COG4_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SMART; SM00762; Cog4; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000029284};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1898..2177
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2177 AA; 236341 MW; 0D9B301BC0FC2BC0 CRC64;
MSWARLQRPG SPGAPLLPVQ NLPIIKTEYN EPDTPHRERS RPTRHHTRSP SSVLKTIADD
YATLTPAETA ARLQSSLTHG LPTSEAFRRL QDHGPNELPH APPEPLWLRF AKQFMEPMIV
LLLCSAGLSL LVGNKDDALS ISIAVTIVVA VAFVQEYRSE KSIEALNHLV PNHAHLIRAE
QPRQPSAAWS PVNEGAPTNG LATDFQDETA VEQASTKVMA STLVPGDLVL FTTGDRIPAD
IRVTKASDLT IDESNLTGEN EPVRVMADAK RRAPSRSPSR ANSYGYNLQP TSQPHPSGPE
IADPDTQSSN RTNIAYMGTL VRSGYGQGIV YATGGQTHFG AIAASVTETE SPRTPLQVSM
DALGAQLSQA SGVFIALIAL VGWFQGKKLL DIFTISISLA VAAIPEGLPI IVTVTLALGV
HRMARHNAIV RRLPSVETLG SVNVVCSDKT GTLTMNHMTT TKMWYFGASK MLDVETDDSE
SSPDSLALRI LRIGNIANNA RVTNLHTASV SASSRAVLSS TKSNHSPSDI LRSRWVGAPT
DVAMMDLVDR YKESDIRDAL GHRLGETPFS SERKWMGVTL PGDRGRDTNS GDREVAYMKG
AIDRVLSRCD TYVTSEGREI VLDSARRQEA LEAAEKLAAE GLRVLAFASG TVPRSARLSA
TSSRSNTPMT KAPLGPHPPA THDEDVYSGL TFAGIVGMSD PPRYGVTKSI STLMKGGVRV
IMITGDAEAT AVAIAKKLGM PVAAPRQHTS SSVAVKPVLR GDEIDDMTDE ELKGAIGSTS
IFARTSPDHK LKIIRALQAR GDIVAMTGDG VNDAPALKKA DIGISMGLHG TDVAKEAADM
ILTDDDFSTI LHAIEEGKGI FSNVQNFLTF QLSTSAAALS LVFICTCLGY RTPLNAMQIL
WINIIMDGPP AQSLGVEPVD ADVMAQPPRR KGAPVLTTTL IQRVLTSAFI IMAGTMLVYT
HEMLDGAVSK RDTTMTFTCF VLFDMFNALS CRSESKSILR GEVGLFSNTL FNWATPQDER
GLFTGTVPVS LVGFTPQPPP MSPLILTNGD RDGAVESPSD APPKAPPNLY ESSTVAEIRA
SLAALHTRDS HITTQLRTLL NSQADLSREL GRLDLLRAHL GTQVVNSRSI SHGMLDSAAR
SAAGLSSKVK ALDLEKTRVE ETLGVVEQVA ELKACVQGVM GSMGAPQDWE AAASYLARAS
KIPEHIITGA FAARIVPSVE IPDPPAVTLE NAKESLCGLF LREFEKAAKE GDGGKVTRFF
KLFPLIGRGE RGLDVYGKYV CGGVSERARA TLRDATGKQI DRDRAGEGKD GFFYANALTK
LFEHIAQIVD GHGGLVERHY GDGRMVRVVE RLQQEADVQG GIVLDTWGDE RGIERRLTDV
KSYPFSFLVQ SFLPSHRAAM GTTRTASPGV GGDANPRRSE DEGVDMKEID GILNETGMML
GRWSLYCRFL ASKTKEPGTS ENAPLSMPPF LTKSALSRKI GSRLTTPFDI FSTFFFRRSV
EKAFQLDETP SGLSLNPSKS LHGQAPYIIS AVDDVMYIVS TVLQRSVSTA QRDVIASVIP
TVGRVLGSDF VGMVQRKMRD ESYPKPAVQG GLPPEDKIIA FIVLINSLDV SNEYISRIIL
TQLKPSEPSA NEAPKTESKL HDLFPFDHDS VFVENTLRNL ETTFSSKTTE LLNEALTVLF
NNVVKPRLRP IISDTFRDID YSLSPGELAD VALAHDLEVD DDAFRLMVPR RFEAGWDALM
RPLQRLMTED TYAQLLESTA THLGRALEKR IMTYAGKVNG VGGVRMERDY AGVVSCVAKG
GSYALRDGFA RGAQVLMVAN MEEDEWEEVL EAEKDGEEGI MWVITPEERA KARGIGGMAS
NMALTTDAIE EETFADYEPE QFYPVHIGDI IQSPRTNYKI IGKLGYGRNS TVWLCLELSD
NIFYTIKIGT AHLNGGNREA AIYEHLQALG SQNVGYGQHY CLVHPPLGVS IDEFQGTFPD
TQYPPIILKA LLNCLFKALD FLHSEAGVIH TDIQARNILL ALDSQSPILN FVAAEKEHPS
ARKVVNDRRS IYVSRCLPES IPPGPPTLCD FGHAIKGSPG AKHSGVIQPL TCRAPEVILG
MAWGAEADIW NLGALTWQLA FGCRLFTGTT EAEQLAAMVA CLGAPPVFLQ RCREEGEARD
TSTRMVYGVA TPSRPRL
//
