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Conserved domains on  [gi|530378972|ref|XP_005248434|]
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sperm flagellar protein 2 isoform X10 [Homo sapiens]

Protein Classification

bifunctional shikimate kinase/3-dehydroquinate synthase; bifunctional nucleoside/nucleotide kinase/histidine phosphatase family protein( domain architecture ID 10533623)

bifunctional shikimate kinase/3-dehydroquinate synthase functions in the shikimate pathway by catalyzing the specific phosphorylation of the 3-hydroxylgroup of shikimic acid using ATP as a cosubstrate and the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate to dehydroquinate| bifunctional nucleoside/nucleotide kinase (NK)/histidine phosphatase (HP) family protein contains an N-terminal NK domain that may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars, and a C-terminal HP domain that contains a conserved His residue that is transiently phosphorylated during the catalytic cycle; similar to Schizosaccharomyces pombe 6-phosphofructo-2-kinase C222.13c

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
 5-97 2.29e-24

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


:

Pssm-ID: 461871  Cd Length: 91  Bit Score: 98.66  E-value: 2.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972     5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294    1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77

                           90
                   ....*....|....
gi 530378972    84 GIITEKPGVATKLL 97
Cdd:pfam06294   78 DLANGKPGAAERLL 91
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 681-863 1.07e-12

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member cd01428:

Pssm-ID: 450170 [Multi-domain]  Cd Length: 194  Bit Score: 68.80  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 760
Cdd:cd01428    44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  761 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 839
Cdd:cd01428   106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170

                         170       180
                  ....*....|....*....|....
gi 530378972  840 PLLEqwFSEPENILIKINAEIDKE 863
Cdd:cd01428   171 PLID--YYKKKGKLVEIDGSGDID 192
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-447 4.18e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  176 EKLERFQKLKEEQRCFDIEKQYLNRRRQNEIMAKIQAAIIQIpkpasNRTLKALEAQkMMKKKKEAEDVADEIKKFEALI 255
Cdd:COG1196   210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL-----EAELEELEAE-LAELEAELEELRLELEELELEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  256 kKDLQAKESASKTSLDTAGQTTTDLLNTYSD-DEYIKKIQKRLEEDAFAREQREKRRRKLLMDQLIAHEAQEEAYREEQL 334
Cdd:COG1196   284 -EEAQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  335 INRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQDALDREAALAKQAK-IDFEEQFLKEKRFHDQI 413
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEeLEEALAELEEEEEEEEE 442

                         250       260       270
                  ....*....|....*....|....*....|....
gi 530378972  414 AVERAQARYEKHYSVCAEILDQIVDLSTKVADYR 447
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
 
Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
 5-97 2.29e-24

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


Pssm-ID: 461871  Cd Length: 91  Bit Score: 98.66  E-value: 2.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972     5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294    1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77

                           90
                   ....*....|....
gi 530378972    84 GIITEKPGVATKLL 97
Cdd:pfam06294   78 DLANGKPGAAERLL 91
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 681-863 1.07e-12

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 68.80  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 760
Cdd:cd01428    44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  761 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 839
Cdd:cd01428   106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170

                         170       180
                  ....*....|....*....|....
gi 530378972  840 PLLEqwFSEPENILIKINAEIDKE 863
Cdd:cd01428   171 PLID--YYKKKGKLVEIDGSGDID 192
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 681-873 1.66e-09

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 59.76  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 760
Cdd:COG0563    45 LGKKAKEYMDAGELVPDEIVIGLVKERLAQPDCANGFILDGFPRTVAQAEALDELLAELGIKL----------------- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  761 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNLR---DQ---IQHRIIG 834
Cdd:COG0563   108 -------------DAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVCDKCGGELVQradDNeetVRKRLEV 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 530378972  835 FLDN-WPLLEqwFSEPENILIKINAEIDKESLCEKVKEIL 873
Cdd:COG0563   175 YHEQtAPLID--YYRKKGKLVEIDGEGSIEEVTADILAIL 212
adk PRK00279
adenylate kinase; Reviewed
 681-790 3.81e-08

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 55.93  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 760
Cdd:PRK00279   45 LGKEAKSYMDAGELVPDEIVIGLVKERLAQPDCKNGFLLDGFPRTIPQAEALDEMLKELGIKL----------------- 107

                          90       100       110
                  ....*....|....*....|....*....|
gi 530378972  761 atskeiplpspafDFVILLDVSDTSSMSRM 790
Cdd:PRK00279  108 -------------DAVIEIDVPDEELVERL 124
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 681-736 1.36e-07

adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273569 [Multi-domain]  Cd Length: 210  Bit Score: 54.16  E-value: 1.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530378972   681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQD-CILDGFPMTLNQAQLLEEAL 736
Cdd:TIGR01351   44 LGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENgFILDGFPRTLSQAEALDALL 100
ADK pfam00406
Adenylate kinase;
680-737 2.00e-05

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 47.30  E-value: 2.00e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530378972   680 QLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALT 737
Cdd:pfam00406   40 ELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFLLDGFPRTVPQAEALEELLE 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-447 4.18e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  176 EKLERFQKLKEEQRCFDIEKQYLNRRRQNEIMAKIQAAIIQIpkpasNRTLKALEAQkMMKKKKEAEDVADEIKKFEALI 255
Cdd:COG1196   210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL-----EAELEELEAE-LAELEAELEELRLELEELELEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  256 kKDLQAKESASKTSLDTAGQTTTDLLNTYSD-DEYIKKIQKRLEEDAFAREQREKRRRKLLMDQLIAHEAQEEAYREEQL 334
Cdd:COG1196   284 -EEAQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  335 INRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQDALDREAALAKQAK-IDFEEQFLKEKRFHDQI 413
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEeLEEALAELEEEEEEEEE 442

                         250       260       270
                  ....*....|....*....|....*....|....
gi 530378972  414 AVERAQARYEKHYSVCAEILDQIVDLSTKVADYR 447
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 101-431 9.13e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 9.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972   101 YIALQKKKKSGLTGVEMQTMQRLTNLRL--QNMKSDTFQERLRHMIPRQTDFNLMRITYRF----QEKYKHVKEDLAhlh 174
Cdd:pfam17380  233 YEKMERRKESFNLAEDVTTMTPEYTVRYngQTMTENEFLNQLLHIVQHQKAVSERQQQEKFekmeQERLRQEKEEKA--- 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972   175 fEKLERFQKLKEEQRCFDIEKQylnrrRQNEIMAKIQAAIIQipkpaSNRTLK--ALEAQKMMKKKKEAEDVADEIKKFE 252
Cdd:pfam17380  310 -REVERRRKLEEAEKARQAEMD-----RQAAIYAEQERMAME-----RERELEriRQEERKRELERIRQEEIAMEISRMR 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972   253 ALIKKDLQAKESASKTSLDTAGQTTTDLLntysDDEYIKKIQKRLEEdafareqrekrrrkllMDQLIAH--EAQEEAYR 330
Cdd:pfam17380  379 ELERLQMERQQKNERVRQELEAARKVKIL----EEERQRKIQQQKVE----------------MEQIRAEqeEARQREVR 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972   331 --EEQLINRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQD--ALDREAALAKQAKIDFEeqflKE 406
Cdd:pfam17380  439 rlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkILEKELEERKQAMIEEE----RK 514

                          330       340
                   ....*....|....*....|....*
gi 530378972   407 KRFHDQIAVERAQARYEKHYSVCAE 431
Cdd:pfam17380  515 RKLLEKEMEERQKAIYEEERRREAE 539
 
Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
 5-97 2.29e-24

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


Pssm-ID: 461871  Cd Length: 91  Bit Score: 98.66  E-value: 2.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972     5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294    1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77

                           90
                   ....*....|....
gi 530378972    84 GIITEKPGVATKLL 97
Cdd:pfam06294   78 DLANGKPGAAERLL 91
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 681-863 1.07e-12

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 68.80  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 760
Cdd:cd01428    44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  761 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 839
Cdd:cd01428   106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170

                         170       180
                  ....*....|....*....|....
gi 530378972  840 PLLEqwFSEPENILIKINAEIDKE 863
Cdd:cd01428   171 PLID--YYKKKGKLVEIDGSGDID 192
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 681-873 1.66e-09

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 59.76  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 760
Cdd:COG0563    45 LGKKAKEYMDAGELVPDEIVIGLVKERLAQPDCANGFILDGFPRTVAQAEALDELLAELGIKL----------------- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  761 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNLR---DQ---IQHRIIG 834
Cdd:COG0563   108 -------------DAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVCDKCGGELVQradDNeetVRKRLEV 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 530378972  835 FLDN-WPLLEqwFSEPENILIKINAEIDKESLCEKVKEIL 873
Cdd:COG0563   175 YHEQtAPLID--YYRKKGKLVEIDGEGSIEEVTADILAIL 212
adk PRK00279
adenylate kinase; Reviewed
 681-790 3.81e-08

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 55.93  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 760
Cdd:PRK00279   45 LGKEAKSYMDAGELVPDEIVIGLVKERLAQPDCKNGFLLDGFPRTIPQAEALDEMLKELGIKL----------------- 107

                          90       100       110
                  ....*....|....*....|....*....|
gi 530378972  761 atskeiplpspafDFVILLDVSDTSSMSRM 790
Cdd:PRK00279  108 -------------DAVIEIDVPDEELVERL 124
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 681-736 1.36e-07

adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273569 [Multi-domain]  Cd Length: 210  Bit Score: 54.16  E-value: 1.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530378972   681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQD-CILDGFPMTLNQAQLLEEAL 736
Cdd:TIGR01351   44 LGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENgFILDGFPRTLSQAEALDALL 100
adk PRK02496
adenylate kinase; Provisional
 675-746 7.25e-06

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 48.59  E-value: 7.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530378972  675 LTTRAQLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLTEV 746
Cdd:PRK02496   40 IKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQPDAANGWILDGFPRKVTQAAFLDELLQEIGQSGERV 111
PLN02674 PLN02674
adenylate kinase
 681-736 1.48e-05

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 48.34  E-value: 1.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 736
Cdd:PLN02674   76 LGIKAKEAMDKGELVSDDLVVGIIDEAMKKPSCQKGFILDGFPRTVVQAQKLDEML 131
ADK pfam00406
Adenylate kinase;
680-737 2.00e-05

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 47.30  E-value: 2.00e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530378972   680 QLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALT 737
Cdd:pfam00406   40 ELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFLLDGFPRTVPQAEALEELLE 97
PRK14526 PRK14526
adenylate kinase; Provisional
 681-736 2.92e-05

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 47.15  E-value: 2.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 736
Cdd:PRK14526   45 LGKEIKQIVENGQLVPDSITIKIVEDKINTIKNNDNFILDGFPRNINQAKALDKFL 100
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-447 4.18e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  176 EKLERFQKLKEEQRCFDIEKQYLNRRRQNEIMAKIQAAIIQIpkpasNRTLKALEAQkMMKKKKEAEDVADEIKKFEALI 255
Cdd:COG1196   210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL-----EAELEELEAE-LAELEAELEELRLELEELELEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  256 kKDLQAKESASKTSLDTAGQTTTDLLNTYSD-DEYIKKIQKRLEEDAFAREQREKRRRKLLMDQLIAHEAQEEAYREEQL 334
Cdd:COG1196   284 -EEAQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972  335 INRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQDALDREAALAKQAK-IDFEEQFLKEKRFHDQI 413
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEeLEEALAELEEEEEEEEE 442

                         250       260       270
                  ....*....|....*....|....*....|....
gi 530378972  414 AVERAQARYEKHYSVCAEILDQIVDLSTKVADYR 447
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 101-431 9.13e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 9.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972   101 YIALQKKKKSGLTGVEMQTMQRLTNLRL--QNMKSDTFQERLRHMIPRQTDFNLMRITYRF----QEKYKHVKEDLAhlh 174
Cdd:pfam17380  233 YEKMERRKESFNLAEDVTTMTPEYTVRYngQTMTENEFLNQLLHIVQHQKAVSERQQQEKFekmeQERLRQEKEEKA--- 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972   175 fEKLERFQKLKEEQRCFDIEKQylnrrRQNEIMAKIQAAIIQipkpaSNRTLK--ALEAQKMMKKKKEAEDVADEIKKFE 252
Cdd:pfam17380  310 -REVERRRKLEEAEKARQAEMD-----RQAAIYAEQERMAME-----RERELEriRQEERKRELERIRQEEIAMEISRMR 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972   253 ALIKKDLQAKESASKTSLDTAGQTTTDLLntysDDEYIKKIQKRLEEdafareqrekrrrkllMDQLIAH--EAQEEAYR 330
Cdd:pfam17380  379 ELERLQMERQQKNERVRQELEAARKVKIL----EEERQRKIQQQKVE----------------MEQIRAEqeEARQREVR 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378972   331 --EEQLINRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQD--ALDREAALAKQAKIDFEeqflKE 406
Cdd:pfam17380  439 rlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkILEKELEERKQAMIEEE----RK 514

                          330       340
                   ....*....|....*....|....*
gi 530378972   407 KRFHDQIAVERAQARYEKHYSVCAE 431
Cdd:pfam17380  515 RKLLEKEMEERQKAIYEEERRREAE 539
PRK14528 PRK14528
adenylate kinase; Provisional
 681-746 2.00e-03

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 41.15  E-value: 2.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLTEV 746
Cdd:PRK14528   46 MGIEAKRYMDAGDLVPDSVVIGIIKDRIREADCKNGFLLDGFPRTVEQADALDALLKNEGKSIDKA 111
AAA_17 pfam13207
AAA domain;
682-736 2.88e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 39.92  E-value: 2.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530378972   682 GAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 736
Cdd:pfam13207   39 LVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVIVDGHPRIKTPAGYLPGLP 93
PRK13808 PRK13808
adenylate kinase; Provisional
 681-736 6.76e-03

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 40.64  E-value: 6.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530378972  681 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 736
Cdd:PRK13808   45 VGLKAKDIMASGGLVPDEVVVGIISDRIEQPDAANGFILDGFPRTVPQAEALDALL 100
 
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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