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Database: UniProt
Entry: F2S621_TRIT1
LinkDB: F2S621_TRIT1
Original site: F2S621_TRIT1 
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
//
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