ID A0A177D7Z5_ALTAL Unreviewed; 548 AA.
AC A0A177D7Z5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Aquaporin-like protein {ECO:0000313|EMBL:OAG15300.1};
GN ORFNames=CC77DRAFT_1013246 {ECO:0000313|EMBL:OAG15300.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG15300.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG15300.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG15300.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377;
CC Evidence={ECO:0000256|ARBA:ARBA00034651};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KV441494; OAG15300.1; -; Genomic_DNA.
DR RefSeq; XP_018380721.1; XM_018523821.1.
DR AlphaFoldDB; A0A177D7Z5; -.
DR STRING; 5599.A0A177D7Z5; -.
DR GeneID; 29109415; -.
DR KEGG; aalt:CC77DRAFT_1013246; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1013246; -.
DR OMA; YEVANPG; -.
DR OrthoDB; 3236018at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR19139:SF199; AQUAPORIN; 1.
DR PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 237..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60898 MW; EB7C4A63B1666102 CRC64;
MAQQNNQQPQ YYGQTLQDGT IMESPVMPPT RASSDSRQEL LRLPAQPHPA HIDYHMESDQ
SLPQQQQQQQ SDLPLRSMPS NARRIGGQSD PNDQWAPNRP RRPSQNVPYT PTTHRGPYIE
DDYEEEDYNP QMYRRRSNRR TQGPPMAYRN YVEQNSRYGP IPRNSVDANM QPQYSDTPGK
PNYEMYYPEQ TDYSPRRPPM PGTGSGGNKG PPEYPSAKAV MRLPWAVWMG SNAKNHFVAF
VGEFVGTTMF LFFAFSGTQV ANIDSSANPD QNTTTNEAAG FSPIVLLYIA LVFAFSLMVN
VWVFFRISGG LFNPAVTFAM LLCRALSPVR AFLLLAAQIT GSIFSSYIVS VLFPTDFNVR
TTLGEGTSLA QGVLIEALLT AELVFTIFML AKEKHKATFI APVGIGLALF IAELVGVYYT
GGSLNPARSF GPCVVTGVFD TEHWIYWVGP AVGAIIAVVF YQFIKILEYE VANPGQDDDD
KDQEVKEEIE KVREGSQEPD LEAQRGPVGG LVSNDGTRTI PTVASIHQIR KKKALEGQGF
GGRGENTY
//
