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Database: UniProt
Entry: A0A3Q0H819_ALLSI
LinkDB: A0A3Q0H819_ALLSI
Original site: A0A3Q0H819_ALLSI 
ID   A0A3Q0H819_ALLSI        Unreviewed;      1000 AA.
AC   A0A3Q0H819;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Zinc finger protein 135-like isoform X1 {ECO:0000313|RefSeq:XP_025068201.1, ECO:0000313|RefSeq:XP_025068202.1};
GN   Name=LOC106722584 {ECO:0000313|RefSeq:XP_025068201.1,
GN   ECO:0000313|RefSeq:XP_025068202.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025068201.1};
RN   [1] {ECO:0000313|RefSeq:XP_025068201.1, ECO:0000313|RefSeq:XP_025068202.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_025068201.1; XM_025212416.1.
DR   RefSeq; XP_025068202.1; XM_025212417.1.
DR   KEGG; asn:106722584; -.
DR   OrthoDB; 4328541at2759; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 17.
DR   Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1.
DR   InterPro; IPR003655; aKRAB.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR16515:SF52; HISTONE-LYSINE N-METHYLTRANSFERASE PRDM9; 1.
DR   PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 12.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 17.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50806; KRAB_RELATED; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          109..188
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000259|PROSITE:PS50804"
FT   DOMAIN          319..383
FT                   /note="KRAB-related"
FT                   /evidence="ECO:0000259|PROSITE:PS50806"
FT   DOMAIN          322..394
FT                   /note="KRAB"
FT                   /evidence="ECO:0000259|PROSITE:PS50805"
FT   DOMAIN          529..556
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          557..584
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          585..612
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          613..640
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          639..666
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          667..694
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          695..722
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          723..750
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          751..778
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          778..805
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          806..833
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          833..860
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          861..888
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          889..916
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          917..944
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          945..972
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          973..1000
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          232..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1000 AA;  112774 MW;  DC8BFF82EC3A564C CRC64;
     MAAALEPVAA VGLPSAVLVQ GEVKMEERDT AGLQAGAEGT GQVHRVLQAG AGELSPRWSA
     PQQVKQQLQE EPVQCQEIQG EEAMQPVQPP PGATQLAPGD VLPTPETWRQ HFRSLRYQEG
     EGPRGVCSRL RELCQRWLEP QRRSKEQILE LVVLEQFLAI LPREMQSWQW GHGVETCAEA
     VALAEGFHLG QAENERLQVT VSVNVEEVSS GTMRPTGDFQ GLVDSCLEHL LEEAGQRETP
     GTRDKPALVP KEDEPPPHQE SGAGTLDRAD QQPPEEEPVN WELQRTSPGR LGERGSLTPD
     LGQVQKRQGR PPKQGESTEL GEVFEAVAVY FTRKEWELLG DEDKVLYRDQ MLRNFHALVS
     LGYGGPTPNL ICRVQQGELE LWVCEDEDHG EISRSEDLSP GGACLLGRAE EQRPEEGPAN
     VEPPQTSPGT LGEMGSLRPE KDQWQKGQEN IAVNQVPSPM GCEIGEETTA RKSPEFRGQF
     VELRGLKSLD HSKIHSGELP HRFIKCAKSF VCSPDLVKHQ HVHREKRRYQ CITCGKTFTQ
     FFSLAQHRHV HLGRKTHRCT KCRKNFICWQ DLSRHRCVQR EEQPHHCTKY GKRFRRPSDL
     AQHRCLHTRE KTHQYSPCGA IFIRSSILAK HQLIHTGQTP CSDSGKSFTR PSHLARHHLV
     HTGENLYQCP ECGKSFTQSS RLAQHQRIHT GEKTLGCPEC GKSFSRSSSL ARHQLIHTGE
     KRHQCSVCGK SFTQSSTLVQ HQRVHTGEKP HRCSECGKSF TQSSSLGRHQ DLHREKAHQC
     LVCGKSFTHS CHLARHQRIH TGEKPYRCSG CGKSFILSSS LARHQRRQAG KADQCLVCGE
     RFTLSCHLAE HQRIHIRKPS HQCSECGKSF TESSSLAQHQ RIHRVERPHQ CSECGKRFTQ
     ASHLARHQLT HTAEKPHRCS ECGKSFTQPY SLSQHQRIHT AEKPYQCSEC GKGFTQSSHL
     ARHQRIHTAE KPYQCSECGR SFTQSSHLAR HQRIHSREHP
//
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