ID D2HIW9_AILME Unreviewed; 840 AA.
AC D2HIW9;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 13-SEP-2023, entry version 64.
DE RecName: Full=Heat shock protein family A (Hsp70) member 4 like {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=PANDA_011198 {ECO:0000313|EMBL:EFB27961.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB27961.1};
RN [1] {ECO:0000313|EMBL:EFB27961.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; GL192894; EFB27961.1; -; Genomic_DNA.
DR RefSeq; XP_019658298.1; XM_019802739.1.
DR RefSeq; XP_019658299.1; XM_019802740.1.
DR AlphaFoldDB; D2HIW9; -.
DR GeneID; 100464340; -.
DR KEGG; aml:100464340; -.
DR CTD; 22824; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; D2HIW9; -.
DR OrthoDB; 276440at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd11738; HSPA4L_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 2.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR042708; HSPA4L_NBD.
DR PANTHER; PTHR45639:SF5; HEAT SHOCK 70 KDA PROTEIN 4L; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT REGION 502..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 840
FT /evidence="ECO:0000313|EMBL:EFB27961.1"
SQ SEQUENCE 840 AA; 94677 MW; 852B2D7FD8682110 CRC64;
MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN AAKSQIVTNV
RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSAG VKVRYLEEER PFAIEQVTGM
LLAKLKETSE NALKKPVADC VISIPSFFTD AERRSVMAAA QVAGLNCLRL MNETTAVALA
YGIYKQDLPP LDEKPRNVIF IDMGHSAYQV SVCAFNKGKL KVLATTFDPY LGGRNFDEAL
VDYFCEEFKT KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK
MNRAQFEQLC ASLFTRVEPP LKAVMEQANL QREDISSIEI VGGATRIPAV KEQITKFFLK
DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY SIMLRWKTSF EDGTGECEVF
CKNHPAPFSK VITFHKKEPF ELEAFYTNLH EVPYPDPRIG SFTIQNVFPQ SDGDSSKVKV
KVRVNIHGIF SVASASVIEK QNVEGDPSDA PMETEASFKN ESKDDVDKMQ VDQEEGGHQK
CHAEHTPEEE IDHTGTKTKS APSDKQDRLN QTIKKGKVKS IDLPIQSSLC RQLGQDLLNS
YIENEGKMIM QDKLEKERND AKNAVEEYVY DFRDKLGTVY EKFITQEDLN KLSAILEDTE
NWLYEEGEDQ PKQIYVDKLQ ELKKYGQPIQ MRYMEHEERP KALNDLGKKI QLVMKVIEAY
RNKDERYDHL DPAEVEKVEK YISEAMSWLN SKMNAQNKLS LTQDPVVKVS EIVAKSKELD
SFCNPIIYKP KPKVEVAEDK AKANSEHNGP MDGQSGTETK PDTTKDSSQH TKSSGEMEVD
//
