NAT1_SCHPO
ID NAT1_SCHPO Reviewed; 729 AA.
AC O74985;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=N-terminal acetyltransferase A complex subunit nat1;
DE Short=NatA complex subunit nat1;
GN Name=nat1; ORFNames=SPCC338.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Non-catalytic component of the NatA N-terminal
CC acetyltransferase, which catalyzes acetylation of proteins beginning
CC with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal
CC eukaryotic translation and processing, protect against proteolytic
CC degradation and protein turnover. nat1 anchors ard1 and nat5 to the
CC ribosome and may present the N termini of nascent polypeptides for
CC acetylation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)
CC complex, which is composed of at least ard1 and nat1. nat1 associates
CC with the nascent polypeptide chain and the ribosome (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC O74985; Q9UTI3: ard1; NbExp=4; IntAct=EBI-16067095, EBI-16067117;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAA19338.1; -; Genomic_DNA.
DR PIR; T41735; T41735.
DR RefSeq; NP_588160.1; NM_001023149.2.
DR PDB; 4KVM; X-ray; 2.60 A; A/B/C/D=1-729.
DR PDB; 4KVO; X-ray; 3.15 A; A/B/C/D=1-729.
DR PDBsum; 4KVM; -.
DR PDBsum; 4KVO; -.
DR AlphaFoldDB; O74985; -.
DR SMR; O74985; -.
DR BioGRID; 275904; 4.
DR DIP; DIP-60548N; -.
DR IntAct; O74985; 1.
DR STRING; 4896.SPCC338.07c.1; -.
DR iPTMnet; O74985; -.
DR MaxQB; O74985; -.
DR PaxDb; O74985; -.
DR PRIDE; O74985; -.
DR EnsemblFungi; SPCC338.07c.1; SPCC338.07c.1:pep; SPCC338.07c.
DR GeneID; 2539338; -.
DR KEGG; spo:SPCC338.07c; -.
DR PomBase; SPCC338.07c; -.
DR VEuPathDB; FungiDB:SPCC338.07c; -.
DR eggNOG; KOG1156; Eukaryota.
DR HOGENOM; CLU_006686_0_0_1; -.
DR InParanoid; O74985; -.
DR OMA; WQEDQFD; -.
DR PhylomeDB; O74985; -.
DR BRENDA; 2.3.1.255; 5613.
DR PRO; PR:O74985; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0031415; C:NatA complex; IDA:PomBase.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:PomBase.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; IC:PomBase.
DR InterPro; IPR021183; NatA_aux_su.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12569; NARP1; 1.
DR PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..729
FT /note="N-terminal acetyltransferase A complex subunit nat1"
FT /id="PRO_0000311768"
FT REPEAT 10..43
FT /note="TPR 1"
FT REPEAT 45..77
FT /note="TPR 2"
FT REPEAT 78..111
FT /note="TPR 3"
FT REPEAT 146..182
FT /note="TPR 4"
FT REPEAT 185..218
FT /note="TPR 5"
FT REPEAT 380..413
FT /note="TPR 6"
FT REPEAT 415..447
FT /note="TPR 7"
FT REPEAT 493..526
FT /note="TPR 8"
FT REPEAT 677..710
FT /note="TPR 9"
FT REGION 626..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 599..635
FT /evidence="ECO:0000255"
FT COMPBIAS 626..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:4KVM"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:4KVO"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 308..324
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:4KVM"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 356..360
FT /evidence="ECO:0007829|PDB:4KVM"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 378..393
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 414..427
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 430..442
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 443..446
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 448..460
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:4KVM"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 482..489
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 493..505
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 509..529
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 533..540
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 543..553
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 554..557
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 560..578
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 588..596
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 601..630
FT /evidence="ECO:0007829|PDB:4KVM"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 651..654
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 658..666
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:4KVM"
FT TURN 673..675
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 678..689
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 693..705
FT /evidence="ECO:0007829|PDB:4KVM"
FT HELIX 712..725
FT /evidence="ECO:0007829|PDB:4KVM"
SQ SEQUENCE 729 AA; 83679 MW; 802AE8F1B203F687 CRC64;
MAKVQLSPKE ITLFRTALKC YETKQYKKGL KAIEPLLERH PEHGESLAIK GILLHSLGNT
KEGYDNVRLG LRNDVGSGVC WHIFGLISRA DKDYVQAAKC YINAHKLEKN NSSLLRDLAL
LQSQLRQYKA LADTRNALLQ DNPGVRANWS ALAVAQFLRG EYASAYKIVD AFESTINQGV
PVDTQEESEA MLFMNLVILK KDGVEDAYKH LLSIEKKVLD RVAFLETRAE YELYLSKMEE
AKSTIYLLLD RNPDNHQYYY NLQRAYGYED ASGKVLDSAE WLNLYSQLAK RYPKSECPTR
LPLEKLEGDE FLTHVDLYLR KKLKRGIPSV FVDVKSLYKD TKKCKVVEDL VSKYASSLST
TNKFSEDDDN SQIEIPTTLL WTYYFLAQHF DHVGELEKAE KYVDLAIDHT PTLVELFMTK
ARISKHKGEL QTAMEIMDHA RKLDLQDRFI NGKCAKYMLR NDENELAAKT VSLFTRNEAV
GGAVGDLADM QCLWYMLEDG KSFARQKKFA LALKRFSTVF KIFDTWADDQ FDFHFFAFRK
GSLRTYLDLM SWEDSVYDDP SFREAAQGSI EIYFALFDLP FAKYSPKLPD FEKLSSGEIN
EEEEKKIYKK LKKDLSKRLE RAEKLKEADK SRAKSEDGMP VKYDEDPLGE NLVATSEPLK
EAQKCLEKLL PYGDKNPSAY ILAAQLYTRL KNFDTASKYL EQAKVILGQN DPTVISTEKF
YNSIKTQSN
