ID V9KSM5_CALMI Unreviewed; 531 AA.
AC V9KSM5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Protein AF-17-like protein {ECO:0000313|EMBL:AFP01350.1};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP01350.1};
RN [1] {ECO:0000313|EMBL:AFP01350.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen {ECO:0000313|EMBL:AFP01350.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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DR EMBL; JW868832; AFP01350.1; -; mRNA.
DR AlphaFoldDB; V9KSM5; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15574; PHD_AF10_AF17; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR049781; AF10/AF17_PHD.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13793:SF162; ALHAMBRA, ISOFORM P; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 5..57
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 62..181
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 117..180
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 193..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 531
FT /evidence="ECO:0000313|EMBL:AFP01350.1"
SQ SEQUENCE 531 AA; 56987 MW; D37AEA2443A7A9EB CRC64;
MKEMVGGCCV CSDERGWTEN PLVYCDGHGC NVAVHQACYG IVQVPTGPWF CRKCESQERA
ARVRCELCPH KDGALKRTDN GGWAHVVCAL YVPEVQFANV ISMEPIVLQY VPHERFNKTC
YLCEEQGRES KAATGACMTC NRHGCRQAFH VTCAQMAGLL CEEQGSEIDN VKYCGYCKYH
FNKVKKSRHS ANSAYDQGLS DSSTHSQDKL SSLHDKQRKS RKDRERPKQR LKKPTESLSV
VVNTVPAATE KGACTPHVSG KEPAAEVNRS ESKVKKASGH GSSQRGRKPG GGKSSSSVPA
ASSTSTFQQG SLLNTPSAPT CQELVRIPKP DVRGETYLQS LCLSQSSPPY ETIKGGDLFS
TDSNLSGFNP LMRYSSGTGG PAKSLESTRG ELRTCSGGMG GPSAGGGGYK RPQTVGAEGE
ETVKEKKHKA NKKSKAGRGR PKGSKNSEPP PALAPPLLAM PEVVTAIGNP TLPKLTPSTC
AMPGMNIESS LLSTAKDLHR LHGTETGHSV QLVHAGVYTP HEPPPVLHSP S
//
