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Database: UniProt
Entry: A0A3Q2ZIW4_KRYMA
LinkDB: A0A3Q2ZIW4_KRYMA
Original site: A0A3Q2ZIW4_KRYMA 
ID   A0A3Q2ZIW4_KRYMA        Unreviewed;      1152 AA.
AC   A0A3Q2ZIW4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   Name=MAN2A2 {ECO:0000313|Ensembl:ENSKMAP00000003591.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000003591.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000003591.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361199};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR   RefSeq; XP_017278530.1; XM_017423041.1.
DR   AlphaFoldDB; A0A3Q2ZIW4; -.
DR   STRING; 37003.ENSKMAP00000003591; -.
DR   Ensembl; ENSKMAT00000003659.1; ENSKMAP00000003591.1; ENSKMAG00000002739.1.
DR   GeneID; 108239965; -.
DR   KEGG; kmr:108239965; -.
DR   CTD; 4122; -.
DR   GeneTree; ENSGT01030000234638; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
DR   InterPro; IPR015341; Glyco_hydro_38_cen.
DR   InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR   InterPro; IPR000602; Glyco_hydro_38_N.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF57; ALPHA-MANNOSIDASE 2X; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          502..588
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1152 AA;  131127 MW;  5D94BBD22AAC600F CRC64;
     MKLRKQVTVC GGAIFCVAVF SLYLMLDRVQ HDPARRQNGG NFPRSQISVL QNRIEQLEQL
     LEENHQIISH IKDSVMELTD TGAVSPSGHL PFRSANGSWV LPFDGRPTFL AVKPQDCQFA
     EGNQAQTDVQ MLDVYSILKF DNPDGGVWKQ GFDITYEPDE WDNEPLQVFV VPHSHNDPGW
     VKTFDKYFTD QTQHILNNMV VKLAEDPRRK FIWSEISFFA KWWESADVYK QEAMRKLILG
     GQLEIVTGGW VMTDEATAHY FAMIDQLIEG HQWLERNLGV TPISGWAVDP FGHSATMPYL
     LKMANLTSML IQRIHYSIKK HFASTRSLEF MWRQAWDTGS STDMFCHMMP FYSYDVPHTC
     GPDPKICCQF DFKRLPGGRI NCPWKVPPKS VVEANVAERA QLLLDQYRKK SKLYRSKVLL
     VPLGDDFRYD KALEWDQQYI NYQKLFDYMN SHPELHVQAQ FGTLTEYFNA VYKAYGVAPG
     SRPSDFPVLS GDFFAYADRE DHYWTGYFTS RPFYKSLDRV IESHLRGAEI LYSLAVANAR
     HVGMEGRYPV SDYALLVDAR RSVGLFQHHD AITGTAKENV VIDYGTKLLR ALIGLKRVII
     NAAHFLVMKN KEFYRFYQTE PFLETDDRRA TQDSMPQRTL IELDPAGPRY LVLFNPIEQE
     RLCTVTVLVN TVRVRVLTED GQTLPVQLSA QWSSGTQMSA EVFEATFMVR LPPLGLAVFH
     LYDSSDSPMT FRSDTVLRLS SRSVTARAED PLPVRSQLTD SQTFYISSQA LTLGFSGTTG
     LLESIKRKDD PQEVKVQMQF MVYGTRPSKD KSGAYLFLPD GKPKPYNQKE PPVVRVVEGP
     LFSEVVAQYQ HFQQTVRIHN VPGVDGLSVD MTTMVDIRDQ TNKELAMRLV TSIQSGDVFY
     TDLNGFQIQP RRHYQKLPLQ GNFYPMPSQM YLQDSHHRLT LHTAQALGVS SLESGQFEVI
     MDRRLMQDDN RGLGQGLKDN KKTANHFRLL LERRSIGNKM MDSATTSFPS IASHMTSAFL
     NHEVLALPVL PKRRGVPPLQ TFAPLKSAVP CDFHLLNLRS IQSQQDALSP SPYTALILHR
     LALDCGFEAQ NLGFNCTTTQ GQLSVSSLFK NVDLHLLQPM SLTLMQSSKP LANDSTISLQ
     PMEISTFRIK LR
//
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