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.

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                  ....*....|....*....|..
gi 2329048388  50 KMFIAARRIQSFWRGYRVRKLL 71
Cdd:cd23767     7 RMNRAATLIQALWRGYKVRKEL 28

IQ (isoleucine-glutamine) motif containing G and D (IQCG and IQCD); IQCG and IQCD belong to the IQ motif-containing protein family which contain a C-terminal conserved IQ (isoleucine-glutamine) motif and a coiled-coil domain. The IQCG protein (also known as DRC9 and CFAP122) is essential for sperm flagellum formation in mice. The IQCD protein (also known as DRC10) is involved in sperm fertilization and the acrosome reaction. Both proteins are components of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility. IQCG and IQCD proteins contain a central coiled-coil domain and a C-terminal IQ (isoleucine-glutamine) motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, that interacts with calmodulin (CaM) in a calcium-independent manner. IQ motif-containing proteins that are known to bind calmodulin (CaM) have a wide diversity of biological functions, and they include neuronal growth proteins, myosins, voltage-operated channels, phosphatases, Ras exchange proteins, sperm surface proteins, Ras Gap-like proteins, spindle-associated proteins, and several proteins in plants.

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                  ....*....|....*....|....*
gi 2329048388  68 RKLLHLRWQSAIAIQRWWRGFRTRH 92
Cdd:cd23766     4 KEQEELELRAAIKIQAWWRGIMVRK 28

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.

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                  ....*....|....*....|..
gi 2329048388  50 KMFIAARRIQSFWRGYRVRKLL 71
Cdd:cd23767     7 RMNRAATLIQALWRGYKVRKEL 28

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.

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                  ....*....|....*....|....*
gi 2329048388  68 RKLLHLRWQSAIAIQRWWRGFRTRH 92
Cdd:cd23766     4 KEQEELELRAAIKIQAWWRGIMVRK 28

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.

                          10        20
                  ....*....|....*....|..
gi 2329048388  50 KMFIAARRIQSFWRGYRVRKLL 71
Cdd:cd23767     7 RMNRAATLIQALWRGYKVRKEL 28

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.

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                  ....*....|....*....|.
gi 2329048388  54 AARRIQSFWRGYRVRKLLHLR 74
Cdd:cd22307   149 AATKIQAFFRGTLVRKLLKAH 169

Myosin heavy chain [General function prediction only];

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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329048388   48 DYKMFIAARRIQSFWRGYRVRKLLHLRWQSAIAIQRWWRGFRTRhilyekveRRLQgiiHEHFHRAAIRIQALFRGWWVR 127
Cdd:COG5022    741 DAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLR--------RLVD---YELKWRLFIKLQPLLSLLGSR 809

                   ..
gi 2329048388  128 KF 129
Cdd:COG5022    810 KE 811