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Conserved domains on  [gi|1034631268|ref|XP_016861218|]
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IQ domain-containing protein F1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Adgb_C_mid-like super family cl41701
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
10-51 3.11e-04

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


The actual alignment was detected with superfamily member cd22307:

Pssm-ID: 412094  Cd Length: 416  Bit Score: 40.23  E-value: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034631268  10 TQTVDNANEKSEKPPENQKKLSDKDTVATKIQAWWRGTLVRR 51
Cdd:cd22307   123 SSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRK 164
 
Name Accession Description Interval E-value
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
10-51 3.11e-04

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 40.23  E-value: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034631268  10 TQTVDNANEKSEKPPENQKKLSDKDTVATKIQAWWRGTLVRR 51
Cdd:cd22307   123 SSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRK 164
 
Name Accession Description Interval E-value
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
10-51 3.11e-04

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 40.23  E-value: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034631268  10 TQTVDNANEKSEKPPENQKKLSDKDTVATKIQAWWRGTLVRR 51
Cdd:cd22307   123 SSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRK 164
IQCG cd23766
IQ (isoleucine-glutamine) motif containing G (IQCG); IQCG, also called dynein regulatory ...
37-53 2.01e-03

IQ (isoleucine-glutamine) motif containing G (IQCG); IQCG, also called dynein regulatory complex protein 9 (DRC9), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ (isoleucine-glutamine) motif and a coiled-coil domain. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The expression of IQCG is reduced in the sperm of human asthenospermia patients whose sperm have reduced mobility. It has also been shown to have a role in the calmodulin-mediated calcium signaling pathway in zebrafish haematopoietic development. The human IQCG gene was first reported to be involved in chromosome translocation in a case of acute lymphoid/myeloid leukemia. It expresses predominantly at mice testis during spermatogenesis which interacts with calmodulin in a calcium-dependent manner in the mouse testis. IQCG knockout mice are sterile due to the total immobility of their spermatozoa.


Pssm-ID: 467744  Cd Length: 40  Bit Score: 34.45  E-value: 2.01e-03
                          10
                  ....*....|....*..
gi 1034631268  37 ATKIQAWWRGTLVRRAL 53
Cdd:cd23766    14 AIKIQAWWRGIMVRKGL 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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