ID A0A1H3IU57_ALLWA Unreviewed; 1494 AA.
AC A0A1H3IU57;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=protein O-GlcNAc transferase {ECO:0000256|ARBA:ARBA00011970};
DE EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
GN ORFNames=SAMN05421644_1486 {ECO:0000313|EMBL:SDY31273.1};
OS Allochromatium warmingii (Chromatium warmingii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=61595 {ECO:0000313|EMBL:SDY31273.1, ECO:0000313|Proteomes:UP000198672};
RN [1] {ECO:0000313|Proteomes:UP000198672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 173 {ECO:0000313|Proteomes:UP000198672};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000256|ARBA:ARBA00005386}.
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DR EMBL; FNOW01000048; SDY31273.1; -; Genomic_DNA.
DR STRING; 61595.SAMN05421644_1486; -.
DR OrthoDB; 7058953at2; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000198672; Unassembled WGS sequence.
DR GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11380; -; 2.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 5.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44835:SF1; PROTEIN O-GLCNAC TRANSFERASE; 1.
DR PANTHER; PTHR44835; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE SPINDLY-RELATED; 1.
DR Pfam; PF13844; Glyco_transf_41; 4.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13432; TPR_16; 4.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 15.
DR SUPFAM; SSF48452; TPR-like; 3.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000198672};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDY31273.1}.
FT REPEAT 41..74
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 204..237
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 238..271
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 272..305
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 309..342
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 421..576
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT DOMAIN 599..777
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT REPEAT 864..897
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 898..931
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 932..965
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 966..999
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1000..1033
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1084..1268
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT DOMAIN 1284..1464
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1494 AA; 170504 MW; 7C1EB7A64E4B77E9 CRC64;
MINTDLTKSI LEKAAAYHQS EQFKLAEKLY WSILEREKNC SEAHLNLGIL ALETNRFEIG
LEHLKQALEI EPSNGNYWFA LAQGFFIAKQ NENALIVIER AKSLGFNTSE IQELLDLVKK
NITSNRSNVD VAKLIPSTRK KMLFQLLRLK KFDAAQVQAY QLIEKYPDDV LGWKVLGTLL
VHKNDINQAK FFLERALQIN SSDAEILNSL GQVYQNLKQY DKALECYQAA TLLRPDLAET
WFNQGQSQQY LKQYQAAIKS YSKAILCRPK YIKAHGNLAA LFLQLGQPEN ALDIYNKLLK
ISTTQEEKSD IFYSQAIALS ELGRLNEALK SLDNALSIKP KFAAAITNRS NILTAQGCPE
EALKGFDFAL TIQPDLMVAQ QNRLMCLNYI SDISIERIIS EHVAFGVFLE KQSKRLPNKE
RDINPNKRLR LGFVSGDFRQ HPVIFFLLPV LEHFDKKNFE IYCYSTSHIE DIYTTKCKNL
VDHWLQADTI DQHELADCIY NDSIDLLIDL SGHTSSNALA VFAAKPAPIQ ITWLGYPNIT
GLKSIDYRLV DQFTDPLKKS DVLHSERLIR LPQSFLCYRP WILLDPLPVA LAPYTKNGYI
TFGSFNNLAK ISSVTLKLWV DILLNVPNSR LKLKSSLVSE QETWTRLVKY FATHNIKNER
LEIQMRTQNY QEHLEAYNEI DIALDTFPYN GTTTTCEALL MGVPVISLAG DRHASRVGAS
LLNQVGLFKL IANSQEEYIR IAKDLAANKT FLTQLRKELR ERLEHSSLCD EVGFTQTLET
TLRHMWHLWC AGKQPEPFNG DTSNFVSKKT HFCSLPQNKI LKYHQTQSPS LSQQDLIINL
FNQEQYDKAE STARQIIETY PKDKLAWKIL GAILVKTNRF QEALTILLEA NRIAPNDSVC
INSLGSALHN LKRFKEALKC FRRAIEIDPN YALAYNNLGT VLGDLGKHQE ALNYYSKALE
ISPQTPEFYC NKGLALHFLR RIEESLTAFE EALKYDPNHV DALNKRGVQL ALIGRYQEAI
NSYDAALAIK PDMVYALNNR SNLLKDQGLL LEAYEGYTKA IYINPNLREA WHNRLFCINY
RSDLSREQIF EAHCEFELKQ ATTIARLPEP IHVNRDPERC LRLGFVSGDF RQHSVSFFLQ
AVLEQLDRQQ FEIFCYMTSR YSDQRTCTFQ ALADSWIEAG QLNMSDLANR IRSDNIDILF
DLSGHTEDNA LLAFAAKPAP IQISWIGYPN TTGLSAMDYR LVDDITDPFN EADTYHSESL
IRLPHGFLCY RPQDAAINIS VESLPCLNND FITFGSFNTL AKVTSLTLDI WSQILLVIPN
SRLLLKNPRA KDAAIWNQVI AQFAKRGISM ERLELLGRVD SHIEHLQQYH RMDIALDTFP
YNGTTTTCEA LFMGVPVITL AGDRHAARVG KSLLTQVGLT DFIADSPEHY VQIATYWASN
RCELSNLRAG LRERLEHSPL RDEVGFTRTL EKVLRQMWCL WCAGKSPQVF EVYP
//
