ID A0A1S3RTS1_SALSA Unreviewed; 704 AA.
AC A0A1S3RTS1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine/arginine repetitive matrix protein 1-like isoform X9 {ECO:0000313|RefSeq:XP_014055696.1};
GN Name=LOC106605011 {ECO:0000313|RefSeq:XP_014055696.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014055696.1};
RN [1] {ECO:0000313|RefSeq:XP_014055696.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014055696.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Necessary for efficient RNA polymerase II transcription
CC elongation past template-encoded arresting sites. The arresting sites
CC in DNA have the property of trapping a certain fraction of elongating
CC RNA polymerases that pass through, resulting in locked ternary
CC complexes. Cleavage of the nascent transcript by S-II allows the
CC resumption of elongation from the new 3'-terminus.
CC {ECO:0000256|ARBA:ARBA00025408}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00649}.
CC -!- SIMILARITY: Belongs to the TFS-II family.
CC {ECO:0000256|ARBA:ARBA00009647}.
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DR RefSeq; XP_014055696.1; XM_014200221.1.
DR AlphaFoldDB; A0A1S3RTS1; -.
DR GeneID; 106605011; -.
DR OrthoDB; 1383197at2759; -.
DR Proteomes; UP000087266; Chromosome ssa05.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd00183; TFIIS_I; 1.
DR CDD; cd13749; Zn-ribbon_TFIIS; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR Gene3D; 1.10.472.30; Transcription elongation factor S-II, central domain; 1.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11477:SF4; TRANSCRIPTION ELONGATION FACTOR A PROTEIN 3; 1.
DR PANTHER; PTHR11477; TRANSCRIPTION FACTOR S-II ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR SMART; SM00510; TFS2M; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR SUPFAM; SSF46942; Elongation factor TFIIS domain 2; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00649}; Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00472}.
FT DOMAIN 5..82
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT DOMAIN 543..659
FT /note="TFIIS central"
FT /evidence="ECO:0000259|PROSITE:PS51321"
FT DOMAIN 662..702
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
FT REGION 83..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 81099 MW; 125979A548F52494 CRC64;
MTREEELIRI AKKLDKMVSR NNTEGALDLL NELKGFNMTL KLLQETRIGM SVNGIRKHCT
DDEVVSLAKI LIKDWKRLLD AARTQSTERP NEMKNGVDSN KSTGFPVRSP LEKDTSHKRL
DVSDSDPESE KKEYSDKRRK EKHNVEHKKD ERAVDLKKER YTEAFKNKRH AEQSKNGKHT
EDARKERHVE HLKEPKKERH FEKSRKERHV QEPKNESHTD EPRRESYKDE LRKERHTEER
RKEIPMYEPP QERPEENHRQ GFERRSVLDD LYPSCYSPPR PPRPPRLPPL VRRMSAEVNK
GVKKEVKKER ERRDSSDTLS PSHPRPIPPS RRPSVKVKKE RKKAPPDPNS PLPPLHPRPS
MPTAAEVKKE RKEPPRISVV RKEPPDPNAP FAPLPLHLHP PPPVKRPSVE VKKEREESSD
YKPVSLKVTS SDHVKKDRKD SDTKVPQKTS VDAKKERKDS TDSKPSHSVK RHSTDSKSDR
KEFHGSKSSH PGPLQRKSST DSIERRGKPE MPKIPTTPTS PMSPSFSSAG VPLSPCLATG
ETIRDKCIEM LAAALRTDDN FKEFGTNCDS MAAEIEDHIY TEMGSTDMKY KNRVRSRISN
LKDPKNPGLR RNVLAGGIEL RRFAIMSAEE MASDELKQLR NNLTKEAIRE HQLSKTSGTI
SDLFQCSKCS KKNCTYNQMQ TRSADEPMTT FVLCNECGNR WKFC
//
