IQ calmodulin-binding motif-containing protein 1 isoform X2 [Mus musculus]
Protein Classification
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 ... |
252-297 | 1.01e-05 | ||
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: 47.55 E-value: 1.01e-05
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| Name | Accession | Description | Interval | E-value | ||
| Adgb_C_mid-like | cd22307 | C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ... |
252-297 | 1.01e-05 | ||
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: 47.55 E-value: 1.01e-05
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| IQ | smart00015 | Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
254-275 | 3.67e-04 | ||
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues. Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 37.69 E-value: 3.67e-04
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| IQ | pfam00612 | IQ calmodulin-binding motif; Calmodulin-binding motif. |
255-275 | 1.12e-03 | ||
IQ calmodulin-binding motif; Calmodulin-binding motif. Pssm-ID: 459869 Cd Length: 21 Bit Score: 36.14 E-value: 1.12e-03
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| Name | Accession | Description | Interval | E-value | ||
| Adgb_C_mid-like | cd22307 | C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ... |
252-297 | 1.01e-05 | ||
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: 47.55 E-value: 1.01e-05
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| IQ | smart00015 | Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
254-275 | 3.67e-04 | ||
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues. Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 37.69 E-value: 3.67e-04
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| IQ | pfam00612 | IQ calmodulin-binding motif; Calmodulin-binding motif. |
255-275 | 1.12e-03 | ||
IQ calmodulin-binding motif; Calmodulin-binding motif. Pssm-ID: 459869 Cd Length: 21 Bit Score: 36.14 E-value: 1.12e-03
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
247-278 | 5.93e-03 | ||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. 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 IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 34.44 E-value: 5.93e-03
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