ID A0A094IBD1_9PEZI Unreviewed; 2134 AA.
AC A0A094IBD1;
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=V502_01161 {ECO:0000313|EMBL:KFZ24367.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ24367.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ24367.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
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:KFZ24367.1}.
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DR EMBL; JPKE01000443; KFZ24367.1; -; Genomic_DNA.
DR STRING; 1420915.A0A094IBD1; -.
DR HOGENOM; CLU_001049_1_0_1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000029308; 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; SFLDS00003; Haloacid_Dehalogenase; 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:UP000029308};
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 1746..2131
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 1050..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1428
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 2134 AA; 231623 MW; 9E4C80B82DB1FB6E 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 TQSNHSPSDI 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
ASLKLELTTT SLTFGGAPLT PPTAPMSPLI LTNGDKDGAA ESPSDAPPKA PPNLYESSTV
AEIRASLAAL HTRDSHITTQ LRTLLNSQAD LSRELGRLDL LRAHLGTQVV NSRSISHGML
DSAARSAAGL SSKVKALDLE KTRVEETLGV VEQVAELKAC VQGVMGSMGA PQDWEAAASY
LARASKIPVH IITGAFAARI VPSVEIPDPP AVTLENAKES LCGLFLREFE KAAKEGDGGK
VTRFFKLFPL IGRGERGLDV YGKYVCGGVS ERARATLRDA TGKQIDRDRA GEGKDGFFYA
NALTKLFEHI AQIVDGHGGL VERHYGDGRM VRVVERLQQE ADVQGGIVLD TWGDERGIER
RLTDVKSYPF SFLVQSFLPS HRAAMGTTRT ASPGVGGDAN PRRSEDEGVD MKEIDGILNE
TGMMLGRWSL YCRFLASKTK EPGTSENAPL SMPPFLTKSA LSRKIGSRLT TPFDIFSTFF
FRRSVEKAFQ LDETPSGLSL NPSKPLQGQA PYIISAVDDV MYIVSTVLQR SVSTAQRDVI
ASVIPTVGRV LGSDFVGMVQ RKMRDESYPK PAVQGGLPPE DKIIAFIVLI NSLDVSNEYI
SRIILTQLKP SEPSANEAPK TESKLHDLFP FDHDSVFVEN TLRNLETTFS SKTTELLNEA
LTVLFNNVVK PRLRPIISDT FRDIDYSLSP GELADVALAH DLEVDDDAFR LMVPRRFEAG
WDALMRPLQR LMTEGTYAQL LESTATHLGR ALEKRIMTYA GKVNGVGGVR MERDYAGVVS
CVAKGGSYAL RDGFARGAQV LMVANMEEDE WEEVLEAERD GEEGITWVIT PEERAKARGI
RHHDLSGPYG QHYCLVHPPL GLSIDEFQGT FPDTQYPPII LKALLNCLFK ALDFLHSEAG
VIHTDVQARN ILLALDSQSP ILNFVAAEKE HPSACKVIND RRSIYVSRCL PESIPPGPPT
LCDFGHAIKG SPGAKHSGVI QPLTYRVPEV ILGMAWGAEE DIWNLGALTW QLAFGCHLFT
GTTEVEQLAA MAACLGAPPV EFVQRCREEG EGARYFDEDG LWSGDAITPA PIDDILEEGE
IEAFIDLLKG MLAWVPEERL TAAELRRHAW LHIG
//
