ID A0A0V0VCQ7_9BILA Unreviewed; 1739 AA.
AC A0A0V0VCQ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=FACT complex subunit SSRP1 {ECO:0000313|EMBL:KRX61137.1};
GN ORFNames=T09_119 {ECO:0000313|EMBL:KRX61137.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX61137.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX61137.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX61137.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the SSRP1 family.
CC {ECO:0000256|ARBA:ARBA00010060}.
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:KRX61137.1}.
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DR EMBL; JYDN01000051; KRX61137.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd21994; HMG-box_SSRP1-like; 1.
DR CDD; cd13230; PH1_SSRP1-like; 1.
DR CDD; cd13231; PH2_SSRP1-like; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 1.10.340.70; -; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 2.30.29.220; Structure-specific recognition protein (SSRP1); 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR048993; SSRP1-like_PH1.
DR InterPro; IPR000969; SSRP1/POB3.
DR InterPro; IPR035417; SSRP1/POB3_N.
DR InterPro; IPR024954; SSRP1_DD.
DR InterPro; IPR038167; SSRP1_sf.
DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF21103; PH1_SSRP1-like; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF50630; Acid proteases; 2.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 524..702
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 881..931
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1625..1689
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 1625..1689
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1467..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1595
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1624
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1739 AA; 196912 MW; 1879B3EA49E8F9E8 CRC64;
MRNNLVNTTT DMKTITHFEE FDTSNPAGWE EYSERLVFFL EANSIREGPK RLAVLCSVCG
LKTYKVYQRF LYHRRLQQPG EGVAAYVAEL RHLAQHCNFG ETLESRLRDQ LRVCRAKSQS
TVKKGAAKPN RYATNSIAVE EEEYRINHLT APNEVIATLP FPDVRVSLNN VVIPMQVDSG
ASLTIISEHT FKRVCLPHQR HLEPFHSVLR DFQGREVDVL GVSSLPVKFS SFTESLXSSK
TFDEVMKLLR NHFMPRPSEV YQRFLYHRRL QQPGEGVAAY VAELRHLAQH CNFGETLESR
LRYQLRVCRA KSQSTVKKGA AKPNRYATNS IAVEEEEYRI NHLTAPNEVI ATLPFPDVCV
SLNNVVIPMQ VDSGASLTII SEHTFKRVCL PHQRHLEPFH SVLRDFQGRE VDVLGVSSLP
VKFSSFTESL PVVVVKGPRR SLLGRNWFKP LGIRLVGVHS VAPTSVQDLI DEYAELFSDT
LGTVKGPPVV LHTDESIPLI QMNARRVPFA LKDRISEELD RLVEQGILEP VQHTTWTTPI
VPVIKNDGSI RICGDYKCTV NKALRKDLYQ IPAVNDILAT LKKGRIFAKL DLAQAYQQLE
VDEASAELQT IITHKGAFKA KRLQFGIASA PGIFQRFMDS LLSNLEGVVP YFDDVLIVAE
SQHELLEVLR RVFDRLRDAG IRLNREKCVF VSNSVEFLGY RIDAEGIHPS EKKVEAMPTP
PISEEHLADR TGKDAVLAPV RNWLEKGWPA ELRSEEFKPF HCRRDELSLH KGCVLWGCRV
VIPLASRESI LTMLHSGHPG IARMKGLARS YVWWPKMDEE IESFVKACAE CQETRHEPAK
NVMDAWPEAT EPWTRIHADF FGLIGGKIFL LVVAGSAHRS IYVFDNGTAF KSAEFLAFMQ
SNGIKHVTTA PFHPSSNGLA ERAVQSTKEA LKRITTGSWS ARLARLLLSQ HSTPDPRSNL
SPADLLMKRK LKTCLDRILP NNAEIAKRKV TPPSHREFKV DDHVFVRSYN QQKKWEKAKI
VKRIDFGCIT MNDFQLEFND VCMENLGFLN PGKIKLSNQS ITFKNTKTGK VEHISANDID
HCHWVRLADS PALKCLLKSG PMYRFGGFKD SDFDRLSAYL KKNWNMELKN IEPCITGTNQ
ATANFIGSVL EFENEGQLLF DIPLANVNNC SSAKNEVIME FNQNDECAVS LMEMRLYISA
DPNTEEDPAE EFKRKIAEKA GFLKESGKEL AVLEQVLCAT PRGRYDIKIY PTMLALHGKT
FDYKIPISSI LRLFLLPHQD GRRMFFVIGL DPPVKQGQTR YHFLIMDILK DDEVDLELGL
PEDVLKEKYN GELPRQLSGP LFEIISRIMK CLVRKQITVP GNFVGHTGTP AVGCAYKSAG
GFLYPLQHGF LYVHKPPVYV RLEEISCINF ARSHVTTKSF DFEIQTKQGN IFTFTSIMKE
EYGKLYDFVV SKGINITNTG KRLETTENLF KGSSDEEGER DHYAEQLKSE AREKEENNEN
DSDESEDSDY DPEKGEVRKN SSESSSSSSD SEASGGSEDE SSDQEEKNKK KTKNVSKKAK
SSSSAESDEE KDDDDSDDDD DDDDDQEEEE EEEYDDEKPK PKKAHNKKAV QPPKPKKQKK
VKEGPKRNKS AYMFYLMENR SKFKKPGMSF ADVSKAAAEQ WKKLKDKSKW ENLAAVDRKR
YLDELKEFKK KGGGNIVATK SSKSSTPVKA SKIKSREIIE DSDSSSDEKM DTSEVSSDE
//
