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Conserved domains on  [gi|1039732648|ref|XP_017169367|]
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androglobin isoform X9 [Mus musculus]

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 ...
 796-966 3.66e-53

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: 191.61  E-value: 3.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 796 IHVCSMTTFVIGDEDIVLPNFEPESYRFTEQSIIIMKAIGNVIANFKDKGKLPAALRDLQAAHYPIPLNNKELTAQHFRV 875
Cdd:cd22307     1 LHLCSDTPFVFGDEETVMPLLTKESVRFTEQASSILKALGNAIQSFGDEEYLPAALKELYRSYCPPLLWSKEDKKEHHKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 876 FHISLWRLMKKSQVAKPPSNFKFAFRAMVFDTDLLDSFSEDVSLAEWVDLKYSTPINEK-EYTSEEIAAAVKIQSMWKGC 954
Cdd:cd22307    81 FNEALYHLLKKALGRKETPDELFALRALFLDPDIGLEYKESPSSSLREIVEPDECDCRTrEPTIEEHEAATKIQAFFRGT 160

                         170
                  ....*....|..
gi 1039732648 955 YVRLLMKARKPD 966
Cdd:cd22307   161 LVRKLLKAHKPG 172
CysPc super family cl00051
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
 200-307 1.58e-12

Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.


The actual alignment was detected with superfamily member cd00044:

Pssm-ID: 469591 [Multi-domain]  Cd Length: 315  Bit Score: 69.67  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 200 NSYGKYVVKLYWMGCWRKITVDDFLPFDeeNNLLLPATSYEF-ELWPMLLSKAIIKLanvdvH--VAHRRELGELTVIHA 276
Cdd:cd00044   106 NYAGIYHFRFWKNGEWVEVVIDDRLPTS--NGGLLFMHSRDRnELWVALLEKAYAKL-----HgsYEALVGGNTAEALED 178

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039732648 277 LTGWLPEVIPLHPAYVDRVWELLKEILPEFK 307
Cdd:cd00044   179 LTGGPTERIDLKSADASSGDNDLFALLLSFL 209
Peptidase_C2 super family cl47577
Calpain family cysteine protease;
90-255 1.89e-03

Calpain family cysteine protease;


The actual alignment was detected with superfamily member pfam00648:

Pssm-ID: 459889 [Multi-domain]  Cd Length: 295  Bit Score: 41.33  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648  90 FEDPE--------GKIELPQSLKVFSWKRPQDfifsrtpvvvkneitfdlfspnehlLCSElmrwiiseiyavWKIFNGG 161
Cdd:pfam00648   1 FEDPEfpaddsslGYPPSPPPPRGVEWKRPKE-------------------------ICSN------------PQFIVDG 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 162 ILSN-YHKGNLGELpilpwkpW-----------EHIysLCKAVKGHVPLFNSY-GKYVVKLYWMGCWRKITVDDFLPFde 228
Cdd:pfam00648  44 ASRFdICQGELGDC-------WllaaiasltlnPKL--LERVVPPDQSFEENYaGIFHFRFWRFGEWVDVVIDDRLPT-- 112

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039732648 229 ENNLLL---PATSYEFelWPMLLSKAIIKL 255
Cdd:pfam00648 113 RNGKLLfvhSRDKNEF--WSALLEKAYAKL 140
 
Name Accession Description Interval E-value
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 796-966 3.66e-53

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: 191.61  E-value: 3.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 796 IHVCSMTTFVIGDEDIVLPNFEPESYRFTEQSIIIMKAIGNVIANFKDKGKLPAALRDLQAAHYPIPLNNKELTAQHFRV 875
Cdd:cd22307     1 LHLCSDTPFVFGDEETVMPLLTKESVRFTEQASSILKALGNAIQSFGDEEYLPAALKELYRSYCPPLLWSKEDKKEHHKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 876 FHISLWRLMKKSQVAKPPSNFKFAFRAMVFDTDLLDSFSEDVSLAEWVDLKYSTPINEK-EYTSEEIAAAVKIQSMWKGC 954
Cdd:cd22307    81 FNEALYHLLKKALGRKETPDELFALRALFLDPDIGLEYKESPSSSLREIVEPDECDCRTrEPTIEEHEAATKIQAFFRGT 160

                         170
                  ....*....|..
gi 1039732648 955 YVRLLMKARKPD 966
Cdd:cd22307   161 LVRKLLKAHKPG 172
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
 200-307 1.58e-12

Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.


Pssm-ID: 238004 [Multi-domain]  Cd Length: 315  Bit Score: 69.67  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 200 NSYGKYVVKLYWMGCWRKITVDDFLPFDeeNNLLLPATSYEF-ELWPMLLSKAIIKLanvdvH--VAHRRELGELTVIHA 276
Cdd:cd00044   106 NYAGIYHFRFWKNGEWVEVVIDDRLPTS--NGGLLFMHSRDRnELWVALLEKAYAKL-----HgsYEALVGGNTAEALED 178

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039732648 277 LTGWLPEVIPLHPAYVDRVWELLKEILPEFK 307
Cdd:cd00044   179 LTGGPTERIDLKSADASSGDNDLFALLLSFL 209
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
 200-300 1.98e-10

Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).


Pssm-ID: 128526  Cd Length: 318  Bit Score: 63.11  E-value: 1.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648  200 NSYGKYVVKLYWMGCWRKITVDDFLPFDeENNLLLPATSYEFELWPMLLSKAIIKLANVDVHvahrreLGELTVIHAL-- 277
Cdd:smart00230  98 NYAGIFHFRFWRFGKWVDVVIDDRLPTY-NGELVFMHSNSRNEFWSALLEKAYAKLNGCYEA------LKGGSTTEALed 170

                           90       100
                   ....*....|....*....|....*.
gi 1039732648  278 -TGWLPEVIPLHPAYVDR--VWELLK 300
Cdd:smart00230 171 lTGGVAESIDLKEASKDPdnLFEDLF 196
Peptidase_C2 pfam00648
Calpain family cysteine protease;
90-255 1.89e-03

Calpain family cysteine protease;


Pssm-ID: 459889 [Multi-domain]  Cd Length: 295  Bit Score: 41.33  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648  90 FEDPE--------GKIELPQSLKVFSWKRPQDfifsrtpvvvkneitfdlfspnehlLCSElmrwiiseiyavWKIFNGG 161
Cdd:pfam00648   1 FEDPEfpaddsslGYPPSPPPPRGVEWKRPKE-------------------------ICSN------------PQFIVDG 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 162 ILSN-YHKGNLGELpilpwkpW-----------EHIysLCKAVKGHVPLFNSY-GKYVVKLYWMGCWRKITVDDFLPFde 228
Cdd:pfam00648  44 ASRFdICQGELGDC-------WllaaiasltlnPKL--LERVVPPDQSFEENYaGIFHFRFWRFGEWVDVVIDDRLPT-- 112

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039732648 229 ENNLLL---PATSYEFelWPMLLSKAIIKL 255
Cdd:pfam00648 113 RNGKLLfvhSRDKNEF--WSALLEKAYAKL 140
 
Name Accession Description Interval E-value
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 796-966 3.66e-53

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: 191.61  E-value: 3.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 796 IHVCSMTTFVIGDEDIVLPNFEPESYRFTEQSIIIMKAIGNVIANFKDKGKLPAALRDLQAAHYPIPLNNKELTAQHFRV 875
Cdd:cd22307     1 LHLCSDTPFVFGDEETVMPLLTKESVRFTEQASSILKALGNAIQSFGDEEYLPAALKELYRSYCPPLLWSKEDKKEHHKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 876 FHISLWRLMKKSQVAKPPSNFKFAFRAMVFDTDLLDSFSEDVSLAEWVDLKYSTPINEK-EYTSEEIAAAVKIQSMWKGC 954
Cdd:cd22307    81 FNEALYHLLKKALGRKETPDELFALRALFLDPDIGLEYKESPSSSLREIVEPDECDCRTrEPTIEEHEAATKIQAFFRGT 160

                         170
                  ....*....|..
gi 1039732648 955 YVRLLMKARKPD 966
Cdd:cd22307   161 LVRKLLKAHKPG 172
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
 200-307 1.58e-12

Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.


Pssm-ID: 238004 [Multi-domain]  Cd Length: 315  Bit Score: 69.67  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 200 NSYGKYVVKLYWMGCWRKITVDDFLPFDeeNNLLLPATSYEF-ELWPMLLSKAIIKLanvdvH--VAHRRELGELTVIHA 276
Cdd:cd00044   106 NYAGIYHFRFWKNGEWVEVVIDDRLPTS--NGGLLFMHSRDRnELWVALLEKAYAKL-----HgsYEALVGGNTAEALED 178

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039732648 277 LTGWLPEVIPLHPAYVDRVWELLKEILPEFK 307
Cdd:cd00044   179 LTGGPTERIDLKSADASSGDNDLFALLLSFL 209
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
 200-300 1.98e-10

Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).


Pssm-ID: 128526  Cd Length: 318  Bit Score: 63.11  E-value: 1.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648  200 NSYGKYVVKLYWMGCWRKITVDDFLPFDeENNLLLPATSYEFELWPMLLSKAIIKLANVDVHvahrreLGELTVIHAL-- 277
Cdd:smart00230  98 NYAGIFHFRFWRFGKWVDVVIDDRLPTY-NGELVFMHSNSRNEFWSALLEKAYAKLNGCYEA------LKGGSTTEALed 170

                           90       100
                   ....*....|....*....|....*.
gi 1039732648  278 -TGWLPEVIPLHPAYVDR--VWELLK 300
Cdd:smart00230 171 lTGGVAESIDLKEASKDPdnLFEDLF 196
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 933-964 8.13e-05

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: 40.60  E-value: 8.13e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039732648 933 EKEYTSEEIAAAVKIQSMWKGCYVRLLMKARK 964
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
Peptidase_C2 pfam00648
Calpain family cysteine protease;
90-255 1.89e-03

Calpain family cysteine protease;


Pssm-ID: 459889 [Multi-domain]  Cd Length: 295  Bit Score: 41.33  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648  90 FEDPE--------GKIELPQSLKVFSWKRPQDfifsrtpvvvkneitfdlfspnehlLCSElmrwiiseiyavWKIFNGG 161
Cdd:pfam00648   1 FEDPEfpaddsslGYPPSPPPPRGVEWKRPKE-------------------------ICSN------------PQFIVDG 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732648 162 ILSN-YHKGNLGELpilpwkpW-----------EHIysLCKAVKGHVPLFNSY-GKYVVKLYWMGCWRKITVDDFLPFde 228
Cdd:pfam00648  44 ASRFdICQGELGDC-------WllaaiasltlnPKL--LERVVPPDQSFEENYaGIFHFRFWRFGEWVDVVIDDRLPT-- 112

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039732648 229 ENNLLL---PATSYEFelWPMLLSKAIIKL 255
Cdd:pfam00648 113 RNGKLLfvhSRDKNEF--WSALLEKAYAKL 140
 
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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