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Conserved domains on  [gi|672071150|ref|XP_008766952|]
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IQ calmodulin-binding motif-containing protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 290-316 1.05e-06

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: 45.23  E-value: 1.05e-06
                         10        20
                 ....*....|....*....|....*..
gi 672071150 290 EEQKLHKAACLIQAYWKGFQTRKRLKK 316
Cdd:cd23767    4 ELQRMNRAATLIQALWRGYKVRKELKK 30
Adgb_C_mid-like super family cl41701
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 239-430 1.76e-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: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150 239 ESHQEI----LILLRLSACYkglRSLLNKQEtlteFSRELRQLVDLLTPKIQQEVEE-QKLHKAacLIQAYWKGFQTRKR 313
Cdd:cd22307   24 ESVRFTeqasSILKALGNAI---QSFGDEEY----LPAALKELYRSYCPPLLWSKEDkKEHHKV--FNEALYHLLKKALG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150 314 LKKLPSAVIALQRSFRakrtkmllelnrqkeeeDLRLRLQLQKqramrlSRESRLSMLEIIHPGQ-VEKYNREIEEKSAL 392
Cdd:cd22307   95 RKETPDELFALRALFL-----------------DPDIGLEYKE------SPSSSLREIVEPDECDcRTREPTIEEHEAAT 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 672071150 393 TIQKHWRGYRERKNFRQQRPSLTEY-KAAVTLQRAVLKF 430
Cdd:cd22307  152 KIQAFFRGTLVRKLLKAHKPGTKENlKVAETLKKIWEKI 190
 
Name Accession Description Interval E-value
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 290-316 1.05e-06

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: 45.23  E-value: 1.05e-06
                         10        20
                 ....*....|....*....|....*..
gi 672071150 290 EEQKLHKAACLIQAYWKGFQTRKRLKK 316
Cdd:cd23767    4 ELQRMNRAATLIQALWRGYKVRKELKK 30
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 239-430 1.76e-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: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150 239 ESHQEI----LILLRLSACYkglRSLLNKQEtlteFSRELRQLVDLLTPKIQQEVEE-QKLHKAacLIQAYWKGFQTRKR 313
Cdd:cd22307   24 ESVRFTeqasSILKALGNAI---QSFGDEEY----LPAALKELYRSYCPPLLWSKEDkKEHHKV--FNEALYHLLKKALG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150 314 LKKLPSAVIALQRSFRakrtkmllelnrqkeeeDLRLRLQLQKqramrlSRESRLSMLEIIHPGQ-VEKYNREIEEKSAL 392
Cdd:cd22307   95 RKETPDELFALRALFL-----------------DPDIGLEYKE------SPSSSLREIVEPDECDcRTREPTIEEHEAAT 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 672071150 393 TIQKHWRGYRERKNFRQQRPSLTEY-KAAVTLQRAVLKF 430
Cdd:cd22307  152 KIQAFFRGTLVRKLLKAHKPGTKENlKVAETLKKIWEKI 190
COG5022 COG5022
Myosin heavy chain [General function prediction only];
293-408 1.02e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.45  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150  293 KLHKAACLIQAYWKGFQTRKRL---KKLPSAVIALQRSFRAkrtkmllelnRQKEEEDLRLRLQLQKQRAMRL--SRESR 367
Cdd:COG5022   743 KLDNIATRIQRAIRGRYLRRRYlqaLKRIKKIQVIQHGFRL----------RRLVDYELKWRLFIKLQPLLSLlgSRKEY 812

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 672071150  368 LSMLEIIHPGQV---------EKYNREIEEKSALTIQKHWRGYRERKNFR 408
Cdd:COG5022   813 RSYLACIIKLQKtikrekklrETEEVEFSLKAEVLIQKFGRSLKAKKRFS 862
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 387-408 4.68e-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: 4.68e-04
                           10        20
                   ....*....|....*....|..
gi 672071150   387 EEKSALTIQKHWRGYRERKNFR 408
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 388-408 1.61e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 36.14  E-value: 1.61e-03
                          10        20
                  ....*....|....*....|.
gi 672071150  388 EKSALTIQKHWRGYRERKNFR 408
Cdd:pfam00612   1 RKAAIKIQAAWRGYLARKRYK 21
 
Name Accession Description Interval E-value
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 290-316 1.05e-06

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: 45.23  E-value: 1.05e-06
                         10        20
                 ....*....|....*....|....*..
gi 672071150 290 EEQKLHKAACLIQAYWKGFQTRKRLKK 316
Cdd:cd23767    4 ELQRMNRAATLIQALWRGYKVRKELKK 30
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 239-430 1.76e-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: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150 239 ESHQEI----LILLRLSACYkglRSLLNKQEtlteFSRELRQLVDLLTPKIQQEVEE-QKLHKAacLIQAYWKGFQTRKR 313
Cdd:cd22307   24 ESVRFTeqasSILKALGNAI---QSFGDEEY----LPAALKELYRSYCPPLLWSKEDkKEHHKV--FNEALYHLLKKALG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150 314 LKKLPSAVIALQRSFRakrtkmllelnrqkeeeDLRLRLQLQKqramrlSRESRLSMLEIIHPGQ-VEKYNREIEEKSAL 392
Cdd:cd22307   95 RKETPDELFALRALFL-----------------DPDIGLEYKE------SPSSSLREIVEPDECDcRTREPTIEEHEAAT 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 672071150 393 TIQKHWRGYRERKNFRQQRPSLTEY-KAAVTLQRAVLKF 430
Cdd:cd22307  152 KIQAFFRGTLVRKLLKAHKPGTKENlKVAETLKKIWEKI 190
COG5022 COG5022
Myosin heavy chain [General function prediction only];
293-408 1.02e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.45  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150  293 KLHKAACLIQAYWKGFQTRKRL---KKLPSAVIALQRSFRAkrtkmllelnRQKEEEDLRLRLQLQKQRAMRL--SRESR 367
Cdd:COG5022   743 KLDNIATRIQRAIRGRYLRRRYlqaLKRIKKIQVIQHGFRL----------RRLVDYELKWRLFIKLQPLLSLlgSRKEY 812

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 672071150  368 LSMLEIIHPGQV---------EKYNREIEEKSALTIQKHWRGYRERKNFR 408
Cdd:COG5022   813 RSYLACIIKLQKtikrekklrETEEVEFSLKAEVLIQKFGRSLKAKKRFS 862
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 387-408 4.68e-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: 4.68e-04
                           10        20
                   ....*....|....*....|..
gi 672071150   387 EEKSALTIQKHWRGYRERKNFR 408
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRYK 23
COG5022 COG5022
Myosin heavy chain [General function prediction only];
284-439 1.36e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.99  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150  284 KIQQEVEEQKL-HKAACLIQAYWKGFQTRKRLKKLPSAVIALQRSFR--------------AKRTKMLLELNRQKEEEDL 348
Cdd:COG5022   830 KKLRETEEVEFsLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRvelaerqlqelkidVKSISSLKLVNLELESEII 909

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672071150  349 RLRLQLQKQRAMRL-SRESRLSMLeiihpgqvEKYNREIEEKSALTIQKHwrGYRERKNFRQQRPSLTEykAAVTLQRAV 427
Cdd:COG5022   910 ELKKSLSSDLIENLeFKTELIARL--------KKLLNNIDLEEGPSIEYV--KLPELNKLHEVESKLKE--TSEEYEDLL 977

                         170
                  ....*....|..
gi 672071150  428 LKFLAKCRKKKK 439
Cdd:COG5022   978 KKSTILVREGNK 989
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 388-408 1.61e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 36.14  E-value: 1.61e-03
                          10        20
                  ....*....|....*....|.
gi 672071150  388 EKSALTIQKHWRGYRERKNFR 408
Cdd:pfam00612   1 RKAAIKIQAAWRGYLARKRYK 21
 
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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