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Conserved domains on  [gi|2462611485|ref|XP_054212815|]
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A-kinase anchoring protein 7 isoform X4 [Homo sapiens]

Protein Classification

AKAP7 2'5' RNA ligase-like domain-containing protein( domain architecture ID 12106234)

AKAP7 (A-kinase anchoring protein 7) 2'5' RNA ligase-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 175-319 6.02e-47

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


:

Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 158.59  E-value: 6.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611485 175 PNYFLSIPITNKEIIKGIKILQNAIIQQDERLAKAM-VSDGSFHITLLVMQLLNEDEVNIGIDALLELKPFIEELLQGKH 253
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLKQLPGLDESLfIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILNGNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611485 254 LTLPFQGIGTFG-----NQVGFVKLAEGDHVNSLLEIAETANRTFQEKGILVGESRS-FKPHLTFMKLSKSP 319
Cdd:pfam10469  81 LSLRFKGLETFNddpsaVRVLYAKVEEDDHSPKLQELADRIIRRFQEAGLLVKENNSrVKLHMTLMNTRYRK 152
 
Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 175-319 6.02e-47

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 158.59  E-value: 6.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611485 175 PNYFLSIPITNKEIIKGIKILQNAIIQQDERLAKAM-VSDGSFHITLLVMQLLNEDEVNIGIDALLELKPFIEELLQGKH 253
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLKQLPGLDESLfIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILNGNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611485 254 LTLPFQGIGTFG-----NQVGFVKLAEGDHVNSLLEIAETANRTFQEKGILVGESRS-FKPHLTFMKLSKSP 319
Cdd:pfam10469  81 LSLRFKGLETFNddpsaVRVLYAKVEEDDHSPKLQELADRIIRRFQEAGLLVKENNSrVKLHMTLMNTRYRK 152
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 177-311 1.97e-06

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 47.72  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611485 177 YFLSIPItNKEIIKGIKILQNAIiqqDERLAKAMVSDGSFHITLLVMQLLNEDEVNIGIDAL----LELKPFieellqgk 252
Cdd:COG1514     3 LFIALPP-PEELREALAALRARL---KAAPGGRWVRPENLHLTLAFLGEVDEERLEALAEALaraaAGAPPF-------- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611485 253 hlTLPFQGIGTFGNQVG---FVKLAEGDhvnSLLEIAETANRTFQEKGILVgESRSFKPHLT 311
Cdd:COG1514    71 --ELRLDGLGAFPRPRPrvlWLGVEPSP---ELLALHRRLRAALARAGLPP-ERRPFVPHVT 126
2_5_ligase TIGR02258
2'-5' RNA ligase; This protein family consists of bacterial and archaeal proteins with two ...
 177-318 1.29e-04

2'-5' RNA ligase; This protein family consists of bacterial and archaeal proteins with two tandem copies of Pfam domain pfam02834. Members for which activity has been measured perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-phyiological substrate: half-tRNA splice intermediates from an intron-containing yeast tRNA. The physiological substrate(s) in prokaryotes may include small 2'-5'-link-containing oligonucleotides, perhaps with regulatory or biosynthetic roles. [Transcription, RNA processing]


Pssm-ID: 274058 [Multi-domain]  Cd Length: 179  Bit Score: 42.27  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611485 177 YFLSIPITNkEIIKGIKILQNAIIQQDErlAKAMVSDGSFHITLLVMQLLNEDEVNIGIDALLELK--PFieellqgkhl 254
Cdd:TIGR02258   3 LFIAIDLPP-EIREQLSRIQRKLKSPLD--GIKWVPPENLHITLKFLGEVDEEQVEELEDALAKIAepPF---------- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611485 255 TLPFQGIGTFGNQ----VGFVKLAEGDHVNSLLEIAETAnrtFQEKGILVgESRSFKPHLTFMKLSKS 318
Cdd:TIGR02258  70 TLKLEGIGVFGNPkrprVLWAGVEQSEELTQLHADLERE---LAKLGFSK-EERPFTPHITLARKKSG 133
 
Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 175-319 6.02e-47

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 158.59  E-value: 6.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611485 175 PNYFLSIPITNKEIIKGIKILQNAIIQQDERLAKAM-VSDGSFHITLLVMQLLNEDEVNIGIDALLELKPFIEELLQGKH 253
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLKQLPGLDESLfIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILNGNP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611485 254 LTLPFQGIGTFG-----NQVGFVKLAEGDHVNSLLEIAETANRTFQEKGILVGESRS-FKPHLTFMKLSKSP 319
Cdd:pfam10469  81 LSLRFKGLETFNddpsaVRVLYAKVEEDDHSPKLQELADRIIRRFQEAGLLVKENNSrVKLHMTLMNTRYRK 152
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 177-311 1.97e-06

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 47.72  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611485 177 YFLSIPItNKEIIKGIKILQNAIiqqDERLAKAMVSDGSFHITLLVMQLLNEDEVNIGIDAL----LELKPFieellqgk 252
Cdd:COG1514     3 LFIALPP-PEELREALAALRARL---KAAPGGRWVRPENLHLTLAFLGEVDEERLEALAEALaraaAGAPPF-------- 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462611485 253 hlTLPFQGIGTFGNQVG---FVKLAEGDhvnSLLEIAETANRTFQEKGILVgESRSFKPHLT 311
Cdd:COG1514    71 --ELRLDGLGAFPRPRPrvlWLGVEPSP---ELLALHRRLRAALARAGLPP-ERRPFVPHVT 126
2_5_ligase TIGR02258
2'-5' RNA ligase; This protein family consists of bacterial and archaeal proteins with two ...
 177-318 1.29e-04

2'-5' RNA ligase; This protein family consists of bacterial and archaeal proteins with two tandem copies of Pfam domain pfam02834. Members for which activity has been measured perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-phyiological substrate: half-tRNA splice intermediates from an intron-containing yeast tRNA. The physiological substrate(s) in prokaryotes may include small 2'-5'-link-containing oligonucleotides, perhaps with regulatory or biosynthetic roles. [Transcription, RNA processing]


Pssm-ID: 274058 [Multi-domain]  Cd Length: 179  Bit Score: 42.27  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462611485 177 YFLSIPITNkEIIKGIKILQNAIIQQDErlAKAMVSDGSFHITLLVMQLLNEDEVNIGIDALLELK--PFieellqgkhl 254
Cdd:TIGR02258   3 LFIAIDLPP-EIREQLSRIQRKLKSPLD--GIKWVPPENLHITLKFLGEVDEEQVEELEDALAKIAepPF---------- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462611485 255 TLPFQGIGTFGNQ----VGFVKLAEGDHVNSLLEIAETAnrtFQEKGILVgESRSFKPHLTFMKLSKS 318
Cdd:TIGR02258  70 TLKLEGIGVFGNPkrprVLWAGVEQSEELTQLHADLERE---LAKLGFSK-EERPFTPHITLARKKSG 133
 
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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