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        30
                 ....*....|....*....|....*....|
gi 530401195 212 AEQEMVRMVRAATLIQALWKGYLVRSLLRS 241
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30

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        30
                 ....*....|....*....|....*....|
gi 530401195 212 AEQEMVRMVRAATLIQALWKGYLVRSLLRS 241
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401195    48 EAKRIMSILDEAIYKVEKENFVIQELKNHLHQVLKFSENSLVRTKQEAEKQQKAdFRASQARVAKIQQEILQLQSQFYNL 127
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-LYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401195   128 VMENREAEQALRKKKYKVE------TEIENWIQKYDTEMGEKQEELEDLDAVHREEKISLEELRRRHKVLVGEFAQIREE 201
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDelaeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394

                          170
                   ....*....|....*
gi 530401195   202 REINSKKRMEAEQEM 216
Cdd:TIGR02168  395 IASLNNEIERLEARL 409

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        30
                 ....*....|....*....|....*....|
gi 530401195 212 AEQEMVRMVRAATLIQALWKGYLVRSLLRS 241
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530401195 194 EFAQIREEREINSKKRMEAEQEMVRMVRAATLIQALWKGYLVRSLLRS 241
Cdd:cd22307  121 SPSSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRKLLKA 168

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401195  90 RTKQEAEKQQKADFRASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVEtEIENWIQKYDTEMGEKQEELED 169
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEE 320

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530401195 170 LDAVHREEKISLEELRRRHKVLVGEFAQIREEREINSKKRMEAEQEMVRMVRAATLIQALWK 231
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382