ID A0A151NRI8_ALLMI Unreviewed; 1044 AA.
AC A0A151NRI8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN Name=SUPT16H {ECO:0000313|EMBL:KYO39320.1};
GN ORFNames=Y1Q_0004781 {ECO:0000313|EMBL:KYO39320.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO39320.1};
RN [1] {ECO:0000313|EMBL:KYO39320.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO39320.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. {ECO:0000256|RuleBase:RU367052}.
CC -!- SUBUNIT: Component of the FACT complex.
CC {ECO:0000256|RuleBase:RU367052}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367052}.
CC Chromosome {ECO:0000256|RuleBase:RU367052}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000256|ARBA:ARBA00010779, ECO:0000256|RuleBase:RU367052}.
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:KYO39320.1}.
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; AKHW03002286; KYO39320.1; -; Genomic_DNA.
DR RefSeq; XP_014465558.2; XM_014610072.2.
DR AlphaFoldDB; A0A151NRI8; -.
DR STRING; 8496.A0A151NRI8; -.
DR GeneID; 102567052; -.
DR KEGG; amj:102567052; -.
DR CTD; 11198; -.
DR eggNOG; KOG1189; Eukaryota.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR048969; SPT16_C.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; CDC68 RELATED; 1.
DR PANTHER; PTHR13980:SF15; FACT COMPLEX SUBUNIT SPT16; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF08644; SPT16; 1.
DR Pfam; PF21091; SPT16_C; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367052};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367052};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367052};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367052};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367052};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU367052};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU367052}.
FT DOMAIN 5..165
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 526..686
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 803..893
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 488..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 928..968
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1044
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 119788 MW; 837B1E84FB5C5ECE CRC64;
MALSLDREAY YRRVRRLYAQ WQKGEEEYGD VDGIVVSVGV DEEIVYAKST ALQTWLFGYE
LTDTIMVFCE DKILFMASKK KVEFLKQLAN SKGGDSIPAL TLLVREKNES NKGNFEKMVE
ALKGSKGGKR IGIFSKDKFP GEFMKSWSDC LSKEGFEKVD ISAVVAYTIA VKEDGELNLM
RKAAAITSEV FNKFFKERVM EIVDADEKVR HSKLAESVEK AIEEKKYLSG ADPSTVEMCY
PPIIQSGGNY NLKFSVVSDK NHMHFGAITC AMGIRYKSYC SNLVRTLMVD PPQDMQDNYT
FLLQLQDEML KEMQHGVKLC DVYAAIMDVV KKQKPELLSK ITKNLGFAMG IEFREGSLVI
NSKNQHRLKK GMVFSINLGF SDLTNKEGKK PEERTYALFI GDTVLVDEEG PATILTAVKK
KVKNVGIFLK NEDEDEEEEE KDEAEDLLGR SSRAALLTER TRNELTAEEK RRAHQQELAA
QLNEEARRRL TEQKGEQQIQ KARKSNVSYK NPSLMPKEPH IREMKIYIDK KYETVIMPVF
GIATPFHIAT IKNISMSVEG DYTYLRINFY CPGSALGRNE GNIFPNPEAT FVKEITYRAS
NMKTPGEQTV PALNLQNAFR IIKEVQKRYK TREAEEKEKE GIVKQDSLVI NLNRSNPKLK
DLYIRPNIAQ KRMQGSLEAH VNGFRFTSVR GDKVDILYNN IKHAVFQPCD GEMIIVLHFH
LKNAIMFGKK RHTDVQFYTE VGEITTDLGK HQHMHDRDDL YAEQMEREMR HKLKTAFKNF
IEKVEALTKE ELEFEVPFRD LGFNGAPYRS TCLLQPTSSA LVNCTEWPPF VVTLDEVELI
HFERVQFHLK NFDMVIVYKD YSKKVTMINA IPVASLDPIK EWLNSCDLKY TEGVQSLNWT
KIMKTIVDDP EGFFEQGGWS FLEPEGEGSD AEMAESESEN EDETFNPSEE EYEEEEEDSD
EDYSSEAEES DYSKESLGSE EESGKDWDEL EEEARKADRE SRYEEEEEQS RSLSRKRKGP
AHRSSRSHGR SPGRRAVPPK KKRK
//
