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Conserved domains on  [gi|1044635741|ref|NP_001316488|]
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mitochondrial import inner membrane translocase subunit TIM50 isoform 2 [Homo sapiens]

Protein Classification

HAD_FCP1-like domain-containing protein( domain architecture ID 11576344)

HAD_FCP1-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 34-149 1.20e-47

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319823  Cd Length: 134  Bit Score: 153.91  E-value: 1.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741  34 PYTLVLELTGVLLHPEWS---------------LATGWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDP- 97
Cdd:cd07521     1 KLTLVLDLDETLVHSTWKpvlsedfkipvlpdgREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDPn 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1044635741  98 HGFISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCKKEAFRLQPYNGV 149
Cdd:cd07521    81 GLFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAI 132
 
Name Accession Description Interval E-value
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 34-149 1.20e-47

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 153.91  E-value: 1.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741  34 PYTLVLELTGVLLHPEWS---------------LATGWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDP- 97
Cdd:cd07521     1 KLTLVLDLDETLVHSTWKpvlsedfkipvlpdgREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDPn 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1044635741  98 HGFISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCKKEAFRLQPYNGV 149
Cdd:cd07521    81 GLFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAI 132
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 35-182 5.85e-45

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 147.77  E-value: 5.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741  35 YTLVLELTGVLLHPEWSLA-------------TGWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDPHG-F 100
Cdd:pfam03031   1 KTLVLDLDETLVHSSFEPPlksdfilpvpgetHGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILDPNGkL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741 101 ISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCKKEAFRLQPYNGVALRPWDGNSDDRVLLDLSAFLKTIAlnGVED 180
Cdd:pfam03031  81 FSHRLYRESCKFEDGVYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFLEGLA--GVDD 158


                  ..
gi 1044635741 181 VR 182
Cdd:pfam03031 159 VR 160
CPDc smart00577
catalytic domain of ctd-like phosphatases;
33-161 5.59e-40

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 134.66  E-value: 5.59e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741   33 PPYTLVLELTGVLLH------PEWSLAT------------GWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDS 94
Cdd:smart00577   1 KKKTLVLDLDETLVHsthrsfKEWTNRDfivpvlidghphGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1044635741   95 VDP-HGFISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCKKEAFRLQPYNGVALRPWDGNSDDR 161
Cdd:smart00577  81 LDPkKYFGYRRLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 59-170 2.07e-23

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


Pssm-ID: 274055  Cd Length: 162  Bit Score: 92.36  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741  59 KKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDPHG-FISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCK 137
Cdd:TIGR02251  42 FKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDRGGkVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNS 121

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1044635741 138 KEAFRLQPYNGVALRPWDGNSDDRVLLDLSAFL 170
Cdd:TIGR02251 122 PYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFL 154
 
Name Accession Description Interval E-value
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 34-149 1.20e-47

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 153.91  E-value: 1.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741  34 PYTLVLELTGVLLHPEWS---------------LATGWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDP- 97
Cdd:cd07521     1 KLTLVLDLDETLVHSTWKpvlsedfkipvlpdgREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDPn 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1044635741  98 HGFISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCKKEAFRLQPYNGV 149
Cdd:cd07521    81 GLFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAI 132
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 35-182 5.85e-45

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 147.77  E-value: 5.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741  35 YTLVLELTGVLLHPEWSLA-------------TGWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDPHG-F 100
Cdd:pfam03031   1 KTLVLDLDETLVHSSFEPPlksdfilpvpgetHGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILDPNGkL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741 101 ISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCKKEAFRLQPYNGVALRPWDGNSDDRVLLDLSAFLKTIAlnGVED 180
Cdd:pfam03031  81 FSHRLYRESCKFEDGVYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFLEGLA--GVDD 158


                  ..
gi 1044635741 181 VR 182
Cdd:pfam03031 159 VR 160
CPDc smart00577
catalytic domain of ctd-like phosphatases;
33-161 5.59e-40

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 134.66  E-value: 5.59e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741   33 PPYTLVLELTGVLLH------PEWSLAT------------GWRFKKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDS 94
Cdd:smart00577   1 KKKTLVLDLDETLVHsthrsfKEWTNRDfivpvlidghphGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1044635741   95 VDP-HGFISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCKKEAFRLQPYNGVALRPWDGNSDDR 161
Cdd:smart00577  81 LDPkKYFGYRRLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 59-170 2.07e-23

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


Pssm-ID: 274055  Cd Length: 162  Bit Score: 92.36  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1044635741  59 KKRPGIETLFQQLAPLYEIVIFTSETGMTAFPLIDSVDPHG-FISYRLFRDATRYMDGHHVKDISCLNRDPARVVVVDCK 137
Cdd:TIGR02251  42 FKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDRGGkVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNS 121

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1044635741 138 KEAFRLQPYNGVALRPWDGNSDDRVLLDLSAFL 170
Cdd:TIGR02251 122 PYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFL 154
 
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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