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Conserved domains on  [gi|20130405|ref|NP_612023|]
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tiny tim 2 [Drosophila melanogaster]

Protein Classification

mitochondrial import inner membrane translocase subunit TIM50 family protein( domain architecture ID 10651834)

mitochondrial import inner membrane translocase subunit TIM50 family protein is an essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane; belongs to the haloacid dehalogenase (HAD) superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPDc smart00577
catalytic domain of ctd-like phosphatases;
208-336 1.82e-49

catalytic domain of ctd-like phosphatases;


:

Pssm-ID: 214729  Cd Length: 148  Bit Score: 164.32  E-value: 1.82e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405    208 PPYTLVLEIKDVLVH------PDWTYET------------GWRFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDA 269
Cdd:smart00577   1 KKKTLVLDLDETLVHsthrsfKEWTNRDfivpvlidghphGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20130405    270 LDPNGCIMYR-LVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSIPRWSGNDNDT 336
Cdd:smart00577  81 LDPKKYFGYRrLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
PRK00771 super family cl32006
signal recognition particle protein Srp54; Provisional
 349-384 4.77e-03

signal recognition particle protein Srp54; Provisional


The actual alignment was detected with superfamily member PRK00771:

Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 39.04  E-value: 4.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 20130405  349 GTSEiDDVREVLQYYNQFSDSLSQFRENQRKLGELM 384
Cdd:PRK00771 398 GTTV-EDVRELLKYYKMMKKAMKQLKKGKGKMGKLM 432
 
Name Accession Description Interval E-value
CPDc smart00577
catalytic domain of ctd-like phosphatases;
208-336 1.82e-49

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 164.32  E-value: 1.82e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405    208 PPYTLVLEIKDVLVH------PDWTYET------------GWRFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDA 269
Cdd:smart00577   1 KKKTLVLDLDETLVHsthrsfKEWTNRDfivpvlidghphGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20130405    270 LDPNGCIMYR-LVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSIPRWSGNDNDT 336
Cdd:smart00577  81 LDPKKYFGYRrLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 210-357 7.08e-48

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: 160.48  E-value: 7.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   210 YTLVLEIKDVLVH-------------PDWTYETGWRFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDALDPNGC- 275
Cdd:pfam03031   1 KTLVLDLDETLVHssfepplksdfilPVPGETHGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILDPNGKl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   276 IMYRLVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSIPRWSGNDNDTTLFELTSFLSVLgtSEIDD 355
Cdd:pfam03031  81 FSHRLYRESCKFEDGVYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFLEGL--AGVDD 158


                  ..
gi 20130405   356 VR 357
Cdd:pfam03031 159 VR 160
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 209-326 2.74e-46

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: 155.45  E-value: 2.74e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405 209 PYTLVLEIKDVLVHPDWT---------------YETGWRFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDALDPN 273
Cdd:cd07521   1 KLTLVLDLDETLVHSTWKpvlsedfkipvlpdgREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDPN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 20130405 274 G-CIMYRLVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSI 326
Cdd:cd07521  81 GlFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAIPI 134
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 211-355 1.92e-24

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: 98.52  E-value: 1.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   211 TLVLEIKDVLVH-----PDWTYETGW-----------RFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDALDPNG 274
Cdd:TIGR02251   3 TLVLDLDETLVHstfkmPKVDADFKVpvlidgkiiqvYVFKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDRGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   275 CIM-YRLVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSIPRWSGNDNDTTLFELTSFLsvLGTSEI 353
Cdd:TIGR02251  83 KVIsRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFL--EGLRFE 160


                  ..
gi 20130405   354 DD 355
Cdd:TIGR02251 161 DD 162
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 349-384 4.77e-03

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 39.04  E-value: 4.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 20130405  349 GTSEiDDVREVLQYYNQFSDSLSQFRENQRKLGELM 384
Cdd:PRK00771 398 GTTV-EDVRELLKYYKMMKKAMKQLKKGKGKMGKLM 432
 
Name Accession Description Interval E-value
CPDc smart00577
catalytic domain of ctd-like phosphatases;
208-336 1.82e-49

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 164.32  E-value: 1.82e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405    208 PPYTLVLEIKDVLVH------PDWTYET------------GWRFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDA 269
Cdd:smart00577   1 KKKTLVLDLDETLVHsthrsfKEWTNRDfivpvlidghphGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20130405    270 LDPNGCIMYR-LVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSIPRWSGNDNDT 336
Cdd:smart00577  81 LDPKKYFGYRrLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 210-357 7.08e-48

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: 160.48  E-value: 7.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   210 YTLVLEIKDVLVH-------------PDWTYETGWRFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDALDPNGC- 275
Cdd:pfam03031   1 KTLVLDLDETLVHssfepplksdfilPVPGETHGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILDPNGKl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   276 IMYRLVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSIPRWSGNDNDTTLFELTSFLSVLgtSEIDD 355
Cdd:pfam03031  81 FSHRLYRESCKFEDGVYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFLEGL--AGVDD 158


                  ..
gi 20130405   356 VR 357
Cdd:pfam03031 159 VR 160
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 209-326 2.74e-46

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: 155.45  E-value: 2.74e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405 209 PYTLVLEIKDVLVHPDWT---------------YETGWRFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDALDPN 273
Cdd:cd07521   1 KLTLVLDLDETLVHSTWKpvlsedfkipvlpdgREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDPN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 20130405 274 G-CIMYRLVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSI 326
Cdd:cd07521  81 GlFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAIPI 134
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 211-355 1.92e-24

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: 98.52  E-value: 1.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   211 TLVLEIKDVLVH-----PDWTYETGW-----------RFKKRPGVDVFLKECAKYFEIVVYTAEQGVTVFPLVDALDPNG 274
Cdd:TIGR02251   3 TLVLDLDETLVHstfkmPKVDADFKVpvlidgkiiqvYVFKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDRGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   275 CIM-YRLVRDSTHFDGGHHVKNLDNLNRDLKRVVVVDWDRNSTKFHPSNSFSIPRWSGNDNDTTLFELTSFLsvLGTSEI 353
Cdd:TIGR02251  83 KVIsRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFL--EGLRFE 160


                  ..
gi 20130405   354 DD 355
Cdd:TIGR02251 161 DD 162
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 234-329 4.15e-06

FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. 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 (hhhhDDppphW). 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 the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031.


Pssm-ID: 131304  Cd Length: 156  Bit Score: 46.50  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130405   234 KKRPGVDVFLKECAKYFEIVVYT------AEQgvtvfpLVDALDPNGCIM-YR-LVRDSthfDGGHHVKNLDNL-NRDLK 304
Cdd:TIGR02250  58 KLRPFLHEFLKEASKLYEMHVYTmgtrayAQA------IAKLIDPDGKYFgDRiISRDE---SGSPHTKSLLRLfPADES 128

                          90       100
                  ....*....|....*....|....*
gi 20130405   305 RVVVVDWDRNSTKFHPSNSFSIPRW 329
Cdd:TIGR02250 129 MVVIIDDREDVWPWHKRNLIQIEPY 153
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 349-384 4.77e-03

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 39.04  E-value: 4.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 20130405  349 GTSEiDDVREVLQYYNQFSDSLSQFRENQRKLGELM 384
Cdd:PRK00771 398 GTTV-EDVRELLKYYKMMKKAMKQLKKGKGKMGKLM 432
 
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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