ID F2S621_TRIT1 Unreviewed; 1074 AA.
AC F2S621;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=PAP/25A associated domain-containing protein {ECO:0000313|EMBL:EGD99020.1};
GN ORFNames=TESG_06380 {ECO:0000313|EMBL:EGD99020.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1] {ECO:0000313|EMBL:EGD99020.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|EMBL:EGD99020.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA Birren B.;
RT "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000256|ARBA:ARBA00008593}.
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DR EMBL; GG698517; EGD99020.1; -; Genomic_DNA.
DR AlphaFoldDB; F2S621; -.
DR HOGENOM; CLU_002806_0_0_1; -.
DR OrthoDB; 170176at2759; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR CDD; cd05402; NT_PAP_TUTase; 1.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF113; POLY(A) RNA POLYMERASE CID11; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 71..115
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 278..333
FT /note="PAP-associated"
FT /evidence="ECO:0000259|Pfam:PF03828"
FT REGION 16..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 118701 MW; C724EA8309132849 CRC64;
MAGAASMRRA WPISEDGCHT PSAVTCSRDE PGPLKEKLET EKEAKLSRDI KELYQKLLPS
PESEERRVKF VRKLEKLLDT QWPGNEIKVN VFGSSGNKLC TSDSDVDICI TTPSKCFEPV
CVLADFLAKS GMERVVCVSH AKVPIVKIWD PELQVACDMN VNNTLALENT RMIKTYVELD
DRIRPLAMLV KHWTKRRILN DAALGGTLSS YTWICLIINF LQTRIPPIVP SLQKRVAQSE
GSTDGSSITS TTSCTSTYSS FDDDVEKLGG FGDDNKSTLG ELLFQFFRYY AHEVDYEKNV
MSVRHGKLIS KEEKGWHLLQ NNRLCVEEPF NTSRNLGNTA DDTSFRGLHQ ELRRAFKAIS
EGNLDECCEQ YEYPPEEERV WERPAPQPRP VITPMPPAHS NTRGGRGGGR GGRNQNHYNN
RGSHGGRRAS SAANRSNMAR HQNAAFAAEI ALQAQQAQHA QYLLHDHLYQ QIQILQAQEQ
ELRMKQAMIS SRGNASLLRQ QYIQFPMVPQ QDSGSPDENS QNRANIMHGQ GPLTTPVRQN
IFFSPSFVTP VNVAAPQPQP QQPSSNTTNP PSPSPSTVTP DTRRNHRRSS ITNSSPRSSL
RAQSQPARPI STCVPNNFST FYATAMAQPE AQYVQQQSAR QSPDSPQRTP TEKDYGFPAT
GPYFVKTGPV DENGISPEYI SYYVGDSPQT QGTYSRRSMA SSYPGHAGLA IRNTGLYNIF
YTPTEYRPIP MPTLDQSNIP LEQLDHMNVH TRVPQQQHYN QQATQPKTQS GQGPLIIDGS
VPANDFRRQS TQDEHSEQFF TPQHSSVHSQ RTSRQDTPNN GSREPSPTEQ LGYDEADSVF
GTPNHEVHQH HPQLNGWTQN IRTSNNPAIN GHIGRLETLS EQLQRFQLSD PAYVPHVDTS
HLVKENGIHT HDQHHHANGG GNGNGNGNGV HHAPVQSQKP ATNSKAAPAK ETGRGTSPTV
KRRGNGPGPD TEHHPNGVSQ KQKPRWHSVS GISSSAIPNA TESREAPKPN GVHTNMKPVS
NGGGHDHTST SNTNNSGGGG WQTTTTKKKN KKGANKPATG AEPLPADESL RKGG
//