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Database: UniProt
Entry: A0A3Q0SG99_AMPCI
LinkDB: A0A3Q0SG99_AMPCI
Original site: A0A3Q0SG99_AMPCI 
ID   A0A3Q0SG99_AMPCI        Unreviewed;       692 AA.
AC   A0A3Q0SG99;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000022077.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000022077.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC         glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00000251,
CC         ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|RuleBase:RU610713}.
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DR   Ensembl; ENSACIT00000022665.1; ENSACIP00000022077.1; ENSACIG00000016859.1.
DR   GeneTree; ENSGT01020000230364; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF20; HYALURONIDASE PH-20; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          87..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   692 AA;  76731 MW;  C59649A3C2491BB1 CRC64;
     MVSVAQKSRG CVPLLLFFTR SIFPFSFFAA LAALTAPIAT TLPVADVNKS ILILPATIST
     LSVQKSPTVS PSQTYFSSPA STSRSLSKLP LKADSNPESS ASETSVPLCN PASHRDVPTS
     PSTSKKIHLP GKKVSASLFS GHCHHTSFYP FQPLKQISWL PSDPCKHLNL SYKTIKPLSH
     KNLQSPQTKS CLYPVSAQKV HLQPANPPKP QSPFSPAPLF LLSNSTLVPS LPQSALKNLL
     SPLSVSSLSA ALTLKTTPPA LSKKSQLPPY KTTSSPPEVT TSRLAPAHLP HATGPLFEHQ
     PFTVTWNIPD LVCNRYNISL DTSPFKGVAT PVPGQFLSLF YTDRLGLYPH IDLKSRKKFH
     GGIPQRANLK AIDPFYLGLA VIDWEEWRPL WDRNWGTKRI YQTLSVAHVM QANLSLTVEQ
     ATVKAKQQFQ EAARNLMSEM LALGRAMRPN YLWGFYLFPN CYNYGWQDLH YTGQCSMEVR
     RQNDELLWLW ESSTALYPSV YLQVAALMVR NRVQEALRVS ALPGWRAAAP VFVYMRPVFV
     DDNKRFLSQR DLISTVGESV AVGASGTVLW GASADYDDQM SCEALSSYLT STLNPYITNV
     TTAAQLCSDF LCRGNGRCVR KNYKSNHYLH LNPESFRVVR IQKRYFVLGS PSLADLKSLS
     RRFNCQCYKG LINTXSHWCI RSGCSHCGVC GV
//
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