ID B5IQK3_9CYAN Unreviewed; 1260 AA.
AC B5IQK3;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Integrins alpha chain {ECO:0000313|EMBL:EDY38720.1};
GN ORFNames=CPCC7001_1599 {ECO:0000313|EMBL:EDY38720.1};
OS Cyanobium sp. PCC 7001.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Cyanobium.
OX NCBI_TaxID=180281 {ECO:0000313|EMBL:EDY38720.1, ECO:0000313|Proteomes:UP000003950};
RN [1] {ECO:0000313|EMBL:EDY38720.1, ECO:0000313|Proteomes:UP000003950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7001 {ECO:0000313|EMBL:EDY38720.1,
RC ECO:0000313|Proteomes:UP000003950};
RA Lily E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS990556; EDY38720.1; -; Genomic_DNA.
DR RefSeq; WP_006910625.1; NZ_DS990556.1.
DR AlphaFoldDB; B5IQK3; -.
DR STRING; 180281.CPCC7001_1599; -.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_269041_0_0_3; -.
DR OrthoDB; 561762at2; -.
DR Proteomes; UP000003950; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1800; -; 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 3.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
DR InterPro; IPR044016; Big_13.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR23221; GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR23221:SF7; PHOSPHATIDYLINOSITOL-GLYCAN-SPECIFIC PHOSPHOLIPASE D; 1.
DR Pfam; PF19077; Big_13; 1.
DR Pfam; PF01839; FG-GAP; 7.
DR Pfam; PF00353; HemolysinCabind; 2.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 7.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 2.
DR PROSITE; PS51470; FG_GAP; 7.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Integrin {ECO:0000313|EMBL:EDY38720.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003950};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 153..225
FT /note="Bacterial Ig-like"
FT /evidence="ECO:0000259|Pfam:PF19077"
FT REGION 78..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1260 AA; 126497 MW; 3960143FC4DECF22 CRC64;
MKPIKLISRI TVDGNRLVLR FKRPANIRGL RGNKRFRIFL NGQRITLSGK PRLSRNRRSL
RLNLASAARF GDSLLVTYKD PRGDQKKGVI QNTKGRDQKT LKNRAATNLT AAPPPPPPAP
APAPAPAPAP APAPPPPDTT PPAAPLITSG DRTTDTTPTI SGTAEAGSTV RLFSGAQLLG
STTAAANGAW AFTPASPFSA GAVVALAATA TDAAGNVSAA AQQTLRLYAP IELSAIANGS
GGFVINGESG GDYSGRSVSA AGDVNGDGLA DLLIGAPYAD PNGQTYAGRS YVVFGKTGTT
AIDLATITAG STDGFVINGE TANDFSGRSV SAAGDVNGDG LADLLIGASR ADSSAGRSYV
VFGTAATTAI ELSAIAEGTG GFVINGENTS DNSGYSVSAA GDVNGDGLAD LLIGAYSADG
LTGRSYVVFG KTGTTAIDLA TITAGSTDGF VINGETANDF SGRSVSAAGD VNGDGLADLL
IGASRADSSA GRSYVVFGTA ATTAIELSAI AEGTGGFVIN GENTSDNSGR SVSAAGDVNG
DGLADLLIGA PYADPNGQTY AGRSYVVFGK TGTTAIDLAA ITAGSTDGFV INGESAGAPP
FFSDSDRSGF SVSAAGDVNG DGLADLLIGA PSADFSSSAG RSYVVFGTTD TSPIELSAIA
AGSGGFVING ESGGDRSGIS VSAAGDVNGD GLADLIIGAE DADSFVGRSY VVFGSTSGAF
FQTAVDQLGT SGDDTLTGTA AAETLVGGDG DDTLSGNGAD VLLGGAGNDT FILTTSMLSA
LTEPLGSGGN INQLARIDGG SGFDTISISA TSEEIPLTTL GLNIIANQGA SAPFSASRLA
SIEQIVFSGS SIGLLFLNPN DISDLSGFNT LNSSSASDLG FSNGSYAFQA IEQRHQLVVS
GDGTDQLFGG SGNWMDQGTV LGPTGTYRVY NESSSATQLI VDEDIIRAGL FLTSPLVLDL
DGGGISTTAP DPAGSLAFDL NADGTPESTG WLSPADAFLV LDRDGDGLIS SGAELFGSST
LLPDGTTARN GFEALAVFDS TGQGGNGDQQ ITADDTIFSS LRLWQDSNGD AISQAEELST
LDAHQITSLS LSYTTTESSS DNGNLIRETS SYTSADGSTA LLADVWFATT TSGSENLDPI
TGLSTTSPTL ASSEPSPAQT EDTTGLSTTS SSTTSSADPI TGEPLTAQPP EEISEPLTTT
ETAATPTSSE SFTSEPLTFT PPPSEPLLTP PSSSRTASSD PFNSQTLASD PLDPNQALVL
//
