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Conserved domains on  [gi|2072355148|ref|XP_042541126|]
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cysteine and histidine-rich domain-containing protein 1 [Dipodomys spectabilis]

Protein Classification

cysteine and histidine-rich domain-containing protein( domain architecture ID 10523069)

cysteine and histidine-rich domain (CHORD)-containing protein is a zinc-binding protein similar to Homo sapiens cysteine and histidine-rich domain-containing protein 1 (CHORDC1) and integrin beta-1-binding protein 2 (ITGB1BP2)

Gene Ontology:  GO:0008270

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
 230-316 1.87e-55

p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains.


:

Pssm-ID: 107238  Cd Length: 87  Bit Score: 175.18  E-value: 1.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 230 CRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEP 309
Cdd:cd06488     1 CRHDWHQTGSHVVVSVYAKNSNPELSVVEANSTVLTIHIVFEGNKEFQLDIELWGVIDVEKSSVNMLPTKVEIKLRKAEP 80


                  ....*..
gi 2072355148 310 MQWASLE 316
Cdd:cd06488    81 GSWAKLE 87
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 3-64 3.07e-38

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


:

Pssm-ID: 461502  Cd Length: 62  Bit Score: 130.33  E-value: 3.07e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2072355148   3 LLCYNRGCGQRFDPEANAEDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRH 64
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 155-216 9.04e-34

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


:

Pssm-ID: 461502  Cd Length: 62  Bit Score: 118.39  E-value: 9.04e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2072355148 155 TSCKNGGCSKTYQGLQSLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTTGKH 216
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
 
Name Accession Description Interval E-value
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
 230-316 1.87e-55

p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains.


Pssm-ID: 107238  Cd Length: 87  Bit Score: 175.18  E-value: 1.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 230 CRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEP 309
Cdd:cd06488     1 CRHDWHQTGSHVVVSVYAKNSNPELSVVEANSTVLTIHIVFEGNKEFQLDIELWGVIDVEKSSVNMLPTKVEIKLRKAEP 80


                  ....*..
gi 2072355148 310 MQWASLE 316
Cdd:cd06488    81 GSWAKLE 87
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 3-64 3.07e-38

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


Pssm-ID: 461502  Cd Length: 62  Bit Score: 130.33  E-value: 3.07e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2072355148   3 LLCYNRGCGQRFDPEANAEDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRH 64
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 155-216 9.04e-34

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


Pssm-ID: 461502  Cd Length: 62  Bit Score: 118.39  E-value: 9.04e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2072355148 155 TSCKNGGCSKTYQGLQSLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTTGKH 216
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 230-306 3.75e-14

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 66.51  E-value: 3.75e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2072355148 230 CRHDWHQTGGEVTISVYAKNSLPELSRVEAN--STLLNVHIVfeGEKEFHQNvKLWGVIDVKRSYVTMTATKIEITMRK 306
Cdd:pfam04969   1 PRYDWYQTLDEVTITIPVKGAGIKKKDVKVNikPRSLKVKIK--GGYELIDG-ELFHPIDPEESSWTIEGKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 231-316 1.85e-13

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 70.20  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 231 RHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPM 310
Cdd:PLN03088  158 RHEFYQKPEEVVVTVFAKGVPAENVNVDFGEQILSVVIEVPGEDAYHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPI 237


                  ....*.
gi 2072355148 311 QWASLE 316
Cdd:PLN03088  238 TWASLE 243
 
Name Accession Description Interval E-value
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
 230-316 1.87e-55

p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains.


Pssm-ID: 107238  Cd Length: 87  Bit Score: 175.18  E-value: 1.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 230 CRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEP 309
Cdd:cd06488     1 CRHDWHQTGSHVVVSVYAKNSNPELSVVEANSTVLTIHIVFEGNKEFQLDIELWGVIDVEKSSVNMLPTKVEIKLRKAEP 80


                  ....*..
gi 2072355148 310 MQWASLE 316
Cdd:cd06488    81 GSWAKLE 87
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 3-64 3.07e-38

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


Pssm-ID: 461502  Cd Length: 62  Bit Score: 130.33  E-value: 3.07e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2072355148   3 LLCYNRGCGQRFDPEANAEDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRH 64
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
 233-316 4.23e-35

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 122.70  E-value: 4.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 233 DWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQW 312
Cdd:cd06466     1 DWYQTDTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGSEYQLELDLFGPIDPEQSKVSVLPTKVEITLKKAEPGSW 80


                  ....
gi 2072355148 313 ASLE 316
Cdd:cd06466    81 PSLE 84
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 155-216 9.04e-34

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


Pssm-ID: 461502  Cd Length: 62  Bit Score: 118.39  E-value: 9.04e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2072355148 155 TSCKNGGCSKTYQGLQSLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTTGKH 216
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 234-316 9.41e-22

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 87.73  E-value: 9.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 234 WHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQ-W 312
Cdd:cd06463     1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGEwW 80


                  ....
gi 2072355148 313 ASLE 316
Cdd:cd06463    81 PRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 230-306 3.75e-14

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 66.51  E-value: 3.75e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2072355148 230 CRHDWHQTGGEVTISVYAKNSLPELSRVEAN--STLLNVHIVfeGEKEFHQNvKLWGVIDVKRSYVTMTATKIEITMRK 306
Cdd:pfam04969   1 PRYDWYQTLDEVTITIPVKGAGIKKKDVKVNikPRSLKVKIK--GGYELIDG-ELFHPIDPEESSWTIEGKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 231-316 1.85e-13

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 70.20  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 231 RHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPM 310
Cdd:PLN03088  158 RHEFYQKPEEVVVTVFAKGVPAENVNVDFGEQILSVVIEVPGEDAYHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAEPI 237


                  ....*.
gi 2072355148 311 QWASLE 316
Cdd:PLN03088  238 TWASLE 243
p23_CS_hSgt1_like cd06489
p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related ...
 233-316 3.44e-10

p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related proteins. hSgt1 is a co-chaperone which has been shown to be elevated in HEp-2 cells as a result of stress conditions such as heat shock. It interacts with the heat shock proteins (HSPs) Hsp70 and Hsp90, and it expression pattern is synchronized with these two Hsps. The interaction with HSP90 has been shown to involve the hSgt1_CS domain, and appears to be required for correct kinetochore assembly and efficient cell division. Some proteins in this subgroup contain a tetratricopeptide repeat (TPR) HSP-binding domain N-terminal to this CS domain, and most proteins in this subgroup contain a Sgt1-specific (SGS) domain C-terminal to the CS domain. The SGS domain interacts with some S100 family proteins. Studies suggest that S100A6 modulates in a Ca2+ dependent manner the interactions of hSgt1 with Hsp90 and Hsp70. The yeast Sgt1 CS domain is not found in this subgroup.


Pssm-ID: 107239  Cd Length: 84  Bit Score: 55.85  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 233 DWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQW 312
Cdd:cd06489     1 DWYQTESQVVITILIKNVKPEDVSVEFEKRELSATVKLPSGNDYSLKLHLLHPIVPEQSSYKILSTKIEIKLKKTEAIRW 80


                  ....
gi 2072355148 313 ASLE 316
Cdd:cd06489    81 SKLE 84
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 234-306 1.75e-08

This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR).


Pssm-ID: 107219  Cd Length: 80  Bit Score: 51.05  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 234 WHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGE-------KEFHQNVKLWGVIDVKRSYVTMTATKIEITMRK 306
Cdd:cd00298     1 WYQTDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEeerersyGEFERSFELPEDVDPEKSKASLENGVLEITLPK 80
p23_NCB5OR cd06490
p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. ...
 233-315 5.44e-06

p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. NCB5OR is widely expressed in human organs and tissues and is localized in the ER (endoplasmic reticulum). It appears to play a critical role in maintaining viable pancreatic beta cells. Mice homozygous for a targeted knockout (KO) of the gene encoding NCB5OR develop an early-onset nonautoimmune diabetes phenotype with a non-inflammatory beta-cell deficiency. The role of NCB5OR in beta cells may be in maintaining or regulating their redox status. Proteins in this group in addition contain an N-terminal cytochrome b5 domain and a C-terminal cytochrome b5 oxidoreductase domain. The gene encoding NCB5OR has been considered as a positional candidate for type II diabetes and other diabetes subtypes related to B-cell dysfunction, however variation in its coding region does not appear not to be a major contributor to the pathogenesis of these diseases.


Pssm-ID: 107240  Cd Length: 87  Bit Score: 43.86  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072355148 233 DWHQTGGEVTISVY--AKNSLPELSRVEANSTLLNVHIVFeGEK----EFHQNVKLWGVIDVKrsyVTMTATKIEITMRK 306
Cdd:cd06490     2 DWFQTDSEVTIVVYtkSKGNPADIVIVDDQQRELRVEIIL-GDKsyllHLDLSNEVQWPCEVR---ISTETGKIELVLKK 77


                  ....*....
gi 2072355148 307 AEPMQWASL 315
Cdd:cd06490    78 KEPEKWTSL 86
 
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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