ID A0A3Q0H8L8_ALLSI Unreviewed; 1892 AA.
AC A0A3Q0H8L8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Myosin light chain kinase, smooth muscle isoform X4 {ECO:0000313|RefSeq:XP_025067927.1};
GN Name=MYLK {ECO:0000313|RefSeq:XP_025067927.1};
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_025067927.1};
RN [1] {ECO:0000313|RefSeq:XP_025067927.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR RefSeq; XP_025067927.1; XM_025212142.1.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05762; IgI_8_hMLCK_like; 1.
DR CDD; cd20973; IgI_telokin-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47633; IMMUNOGLOBULIN; 1.
DR Pfam; PF16620; 23ISL; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 9.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 9.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 9.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000313|RefSeq:XP_025067927.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|RefSeq:XP_025067927.1}.
FT DOMAIN 37..126
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 165..253
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 438..526
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 530..622
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 646..734
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 744..839
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1080..1156
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1220..1308
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1316..1409
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1446..1701
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1786..1875
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 257..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1892 AA; 209843 MW; 0CB82923F78ADC39 CRC64;
MSVIMGDVKL VTSARISKTS LTLEPSPLSP SVPTEAPAFT LPPRNIRVQL GSTARFEGKV
RGYPEPQITW YRNGHPVPEG EHYVVDRSIR GIFSLVIKGV QEGDGGKYTC EAANDGGVRQ
VTVELTVEGS CLKRYSLPSG AKTPGGRFSV PAVENRPSIW GESPPKFATK PTRVIVREGQ
TGKFSCKITG RPQPQVTWFK GEIQLQQNDH FNMFEKAGIQ VLEIQNVQLA DAGVYTCTVM
NSAGKASVST ELTVQGSDKT EVHVHPSRPP SKSTTPTAKG VENSDFTRMT SNGIAKELKS
SSTELAVETK EKTTMKKEAC YTFSKDAKDY RQGQLRETSM QPAQEPKGEI RGSQVLQKTS
STITLQAIKV QPEPKAETKS TVTGQSEERK RATQPHMTTR QSVPLAGQAN PRSRYAEHRV
GTRKSITEDK QEPQGFLPQF EICPQSQEAL EGQEVKFKSK VSGKPKPDVE WFKAGAPLKT
RDGVQIYEED GIHCLCLMKA SLGDSGSYSC AAFNPKGRTS TSWALSVKRP KVEEVTPCFS
SILKGCTVSE GQDFVLQCSV EGIPMPQITW LLNDQPIQYA HSTFEEGVAK LTVQDALPED
DGIYTCLAEN SAGRASCSAQ VTVKEKKSST KVEGTQAIQP NKNFAPVFLK GLTDLKVMDG
SQVIMTVEVS ANPPPEIIWL HNGKEIQETE DFHFEKKGSE YSLYIQEVFP EDTGKYTCEA
WNDLGETQTH ATLTVQEPQD GIQPWFISKP RSVTAAPGQN VLISCAIAGD PFPTVHWFKN
GQEIKPGTGC EMLQNEDIFT LVLRNVQPRH AGQYEIHLRN QVGECSCQVS LMLRESSVSK
GETHRDGREP ASSGERRDGG DRGALTFGKA SSLRRNSGET RAAEEEWEDV RGVLKRRVET
REHTEENLRQ QEAEQLDFRD ILGKKVCTKS FSEEDLKEIP AEQMDFRANL QRQVKPKTLS
EEERKVHSPQ QVDFRAVLAK KGTPKAPVPE KASAPKPATP DFRSVLASKK KPPAENGSTD
IQAQNARTNS EVPNAIAEAE TQPSEPVVKE EENDRNCEHG CSMVDGGIIV PEVESKGIAP
SFTEKLQDTH VIEGEKLVLQ CRISSDPAAS VTWTLDDKAI KSSKFIVISQ EESLCSLTIE
KALPEDEGQY KCIAENAAGR SECVCSVLVD EPSPTKTPKP TEKKTKKPKS SLPLVLATES
EATVKKKPAP KTPPKAVLPP QITQFPEDRK VRAGESVELF CKVVGTAPIT CIWMKFRKQI
QESEYIKIEN AENSSKLTIS STKQEHCGCY TLVVENKVGS RQAQVNLTVV DKPDPPAGRP
CASDIRSSSL TLSWYGSSYD GGSAVQSYTV EVWNSADNQW TDLTTCRSTS YNVQDLLADR
EYKFRVRAAN VYGISEPSQE SELVKVGEKP EEPKDEAELS DDEGKEIEID YRTVSINTEQ
KVAEFYNIEE RLGSGKFGQV FKLVEKKTGK VWAGKFFKAY SAKDKENIRQ EIGIMNCLHH
PKLVQCVDAF EEKANIVMVL EIVSGGELFE RIIDEDFELT ERECIKYMKQ ISEGVQYIHK
QGIVHLDLKP ENIMCVNKTG TSIKLIDFGL ARRLETAGSL KVLFGTPEFV APEVINYEPI
GYATDMWSIG VICYILVSGL SPFMGDNDNE TLANVTSATW DFDDEAFDEI SDDAKDFISN
LLKKDMKSRL DCTKCLQHPW LQKDTKTMEA KKLSKDRMKK YMARRKWQKT GHAVRAIGRL
SSMAMISGLS GRKASASSPT SPINTEKIEN EDFLEEVVEE KPHVKPYFTK TILDIEVVEG
SAARFDCKIE GYPDPEVIWY KDDQSIKESR HFQIDYDEDG NCSLTISEVC GDDDAKYTCK
AVNSLGEATC TADLLVETMG KEGEEEEEEE EE
//
