ID A0A099ZGC5_TINGU Unreviewed; 1773 AA.
AC A0A099ZGC5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE SubName: Full=ATPase family AAA domain-containing protein 5 {ECO:0000313|EMBL:KGL79870.1};
DE Flags: Fragment;
GN ORFNames=N309_09143 {ECO:0000313|EMBL:KGL79870.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL79870.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL79870.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL79870.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL892480; KGL79870.1; -; Genomic_DNA.
DR STRING; 94827.A0A099ZGC5; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23389:SF21; ATPASE FAMILY AAA DOMAIN-CONTAINING PROTEIN 5; 1.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053641}.
FT DOMAIN 1069..1293
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 157..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL79870.1"
FT NON_TER 1773
FT /evidence="ECO:0000313|EMBL:KGL79870.1"
SQ SEQUENCE 1773 AA; 198666 MW; A67BB802602CAB7B CRC64;
PCKKRREEDA SVETITRYFS PLAKPADKVL SPPKPNNILD YFKKTSVSEK ASPPVIAGEN
KTQLDADDKY CNSPLKQPSK LRRKGKRINL NNKLREMKDS ENDCVIAICS DDSSRETTGP
RQGANDFTAT CTSADQNCAK ELAEGSLQSE NISDNVINRK NAKKVGSEIN GMKNSVRKSR
KRKHKVNMDL CESLSSENQL NENPRKEPKH QKKVVSPKIE CEVTISDSSV DVQVDDKPAQ
VNESIITVSF EDFLKSQGED SIDHDGEGTT LDNSVTANEA VKTDSISDPE KCEEQQLPLK
TVTVLAQVHS VPPKSPSLHM EQKACRKLAS IFWKQKGCVG EKESRLLPSE SEQTEQTTQK
RKSNVVIEEE DLELAVLETA GSESSRAKCS AEERHQFMKA FRQPPSDVIK TGVKKAPGKL
KQTLTKPSKE GAGGGDLASN KGLGSEITED YVDKHSPCSP ENNRTKNKRA KKLQKNGKGR
KKALKSKDMS VSNTSDPSKD ECSEANAHTK DDALGVRISP SPKVSELRRS SRQKKIETSK
TVTPKKNRIK NTLCENELSD SPLQTSTPKA SKKSLKKNNV YKAEVITIPF EANSPIRMRF
TRINASKKSN KAEAMKNEDL ASKNTKVSSK SISKAKQLVE KAKARRHQGA KARGDAAPVR
RSSRQRALAE RRKVQDGGES VIILDSSLSN ITTAARGVKQ KQKNLRNLND VLGKKSQNIK
ATKNSNGKPG CPPSFLGKNV KKSPDEPIVI FDESSQDASE NSQDGDQFRA KREFLMSGLP
ELLKRQIAKK AAVLEAYCAA GSCFRTVVHV QQKDECYPLW KLKSPSCPVL TRLRKLDTKV
TNVPNIPISL GEFSTVNSKL SGDHSAPVVS IFKLFFFPEV LRKHLLDEIM FSNSQFPVRK
YFYKLLKKQT EQLLFGNSIQ ENSSSTVKSE VNQKHSENWK ETKRKRKETE DRKSKRTKRI
EDSEAEIKSR AARSLSAPIA LSETNVIAGV EKEDVLWTEK YQPQDSSELV GNKKEIEKLH
SWLKEWKKRA DWEEKRNQKG AKEDKDHQDS LDSLDFKNDK SDIEEETSLC NTVLITGPPG
VGKTAAVYAC AQELGFKIFE VNASCQRSGR QILSQLKEAT QSHQVDKKGV NAHRPCFFNS
CSSAKSPKKM YSPKKALSPR KPPLSPRGAK RSLPPKTLAN YFKISSKRKN NDEIITSQEK
NKENNQDSCE EKKDAETKSV KEVEGGEDNR KSATSLILFE EVDIIFDEDA GFLNAIKTFM
ATAKRPIILT TNDPTFSLMF DGYFEEINFR TPSLVNAASY LQVLCLAENL RTDVKDLAAL
LTTNNCDIRQ SVLFLQFWIR SGGGYLKDKH LALHGGDETN KTDEVINSER TTDSKADFSQ
ADTQLPEIPK CDTGCVETLL GLKNILLPSE DLLTFLKHKI TTMDEWNKVI RLLTEFQMKK
VDFIYSNLEF ILPLPVHFVP KQSEASNPIL ERTTVVSSNN KSINSSCPGK SSTGKKSKKT
KNQKRLDILD DSDLFDTGLN YSAEFITLPS DSPVSCVEVK KEELKRMDKE EKMEIKRKTS
EERSALVFQC LNSLTEFVEN MSFLDCCINT NTREPLEFSK DEGFNWTNGK IKNGLSDEFS
VENTDWWRFQ SCSELKATIE ALSFHKCSHN ISKDLEASLG ASRTPESEEL DGLTLHLPNT
RNSVSLSQSA ASSIHKKARK RLAVIRTVFS RTPLNLGNKQ ASIVEYLPTL RNICRSEKLK
EQGKTKRRFL HYLEGIHLEI SRQTINSLSF EFP
//
