|
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 |
2.23e-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: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294 1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77
|
90
....*....|....
gi 145699133 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 ... |
686-868 |
1.26e-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: 68.42 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 765
Cdd:cd01428 44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 766 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 844
Cdd:cd01428 106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170
|
170 180
....*....|....*....|....
gi 145699133 845 PLLEqwFSEPENILIKINAEIDKE 868
Cdd:cd01428 171 PLID--YYKKKGKLVEIDGSGDID 192
|
|
| Smc super family |
cl34174 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-447 |
4.79e-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: 48.39 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 176 EKLERFQKLKEEQRCFDIEKQYLNRRRQNEIMAKIQAAIIQIpkpasNRTLKALEAQkMMKKKKEAEDVADEIKKFEALI 255
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL-----EAELEELEAE-LAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 256 kKDLQAKESASKTSLDTAGQTTTDLLNTYSD-DEYIKKIQKRLEEDAFAREQREKRRRKLLMDQLIAHEAQEEAYREEQL 334
Cdd:COG1196 284 -EEAQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 335 INRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQDALDREAALAKQAK-IDFEEQFLKEKRFHDQI 413
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEeLEEALAELEEEEEEEEE 442
|
250 260 270
....*....|....*....|....*....|....
gi 145699133 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 |
2.23e-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: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294 1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77
|
90
....*....|....
gi 145699133 84 GIITEKPGVATKLL 97
Cdd:pfam06294 78 DLANGKPGAAERLL 91
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
686-868 |
1.26e-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: 68.42 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 765
Cdd:cd01428 44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 766 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 844
Cdd:cd01428 106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170
|
170 180
....*....|....*....|....
gi 145699133 845 PLLEqwFSEPENILIKINAEIDKE 868
Cdd:cd01428 171 PLID--YYKKKGKLVEIDGSGDID 192
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
686-878 |
1.81e-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: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 765
Cdd:COG0563 45 LGKKAKEYMDAGELVPDEIVIGLVKERLAQPDCANGFILDGFPRTVAQAEALDELLAELGIKL----------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 766 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNLR---DQ---IQHRIIG 839
Cdd:COG0563 108 -------------DAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVCDKCGGELVQradDNeetVRKRLEV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 145699133 840 FLDN-WPLLEqwFSEPENILIKINAEIDKESLCEKVKEIL 878
Cdd:COG0563 175 YHEQtAPLID--YYRKKGKLVEIDGEGSIEEVTADILAIL 212
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
686-795 |
4.04e-08 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 55.54 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 765
Cdd:PRK00279 45 LGKEAKSYMDAGELVPDEIVIGLVKERLAQPDCKNGFLLDGFPRTIPQAEALDEMLKELGIKL----------------- 107
|
90 100 110
....*....|....*....|....*....|
gi 145699133 766 atskeiplpspafDFVILLDVSDTSSMSRM 795
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 ... |
686-741 |
1.51e-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: 53.78 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQD-CILDGFPMTLNQAQLLEEAL 741
Cdd:TIGR01351 44 LGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENgFILDGFPRTLSQAEALDALL 100
|
|
| ADK |
pfam00406 |
Adenylate kinase; |
685-742 |
2.20e-05 |
|
Adenylate kinase;
Pssm-ID: 395329 [Multi-domain] Cd Length: 184 Bit Score: 46.92 E-value: 2.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 145699133 685 QLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALT 742
Cdd:pfam00406 40 ELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFLLDGFPRTVPQAEALEELLE 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-447 |
4.79e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 176 EKLERFQKLKEEQRCFDIEKQYLNRRRQNEIMAKIQAAIIQIpkpasNRTLKALEAQkMMKKKKEAEDVADEIKKFEALI 255
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL-----EAELEELEAE-LAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 256 kKDLQAKESASKTSLDTAGQTTTDLLNTYSD-DEYIKKIQKRLEEDAFAREQREKRRRKLLMDQLIAHEAQEEAYREEQL 334
Cdd:COG1196 284 -EEAQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 335 INRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQDALDREAALAKQAK-IDFEEQFLKEKRFHDQI 413
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEeLEEALAELEEEEEEEEE 442
|
250 260 270
....*....|....*....|....*....|....
gi 145699133 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 |
1.45e-03 |
|
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: 43.57 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 101 YIALQKKKKSGLTGVEMQTMQRLTNLRL--QNMKSDTFQERLRHMIPRQTDFNLMRITYRF----QEKYKHVKEDLAhlh 174
Cdd:pfam17380 233 YEKMERRKESFNLAEDVTTMTPEYTVRYngQTMTENEFLNQLLHIVQHQKAVSERQQQEKFekmeQERLRQEKEEKA--- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 175 fEKLERFQKLKEEQRCFDIEKQylnrrRQNEIMAKIQAAIIQipkpaSNRTLK--ALEAQKMMKKKKEAEDVADEIKKFE 252
Cdd:pfam17380 310 -REVERRRKLEEAEKARQAEMD-----RQAAIYAEQERMAME-----RERELEriRQEERKRELERIRQEEIAMEISRMR 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 253 ALIKKDLQAKESASKTSLDTAGQTTTDLLntysDDEYIKKIQKRLEEdafareqrekrrrkllMDQLIAH--EAQEEAYR 330
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKIL----EEERQRKIQQQKVE----------------MEQIRAEqeEARQREVR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 331 --EEQLINRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQD--ALDREAALAKQAKIDFEeqflKE 406
Cdd:pfam17380 439 rlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkILEKELEERKQAMIEEE----RK 514
|
330 340
....*....|....*....|....*
gi 145699133 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 |
2.23e-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: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294 1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77
|
90
....*....|....
gi 145699133 84 GIITEKPGVATKLL 97
Cdd:pfam06294 78 DLANGKPGAAERLL 91
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
686-868 |
1.26e-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: 68.42 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 765
Cdd:cd01428 44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 766 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 844
Cdd:cd01428 106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170
|
170 180
....*....|....*....|....
gi 145699133 845 PLLEqwFSEPENILIKINAEIDKE 868
Cdd:cd01428 171 PLID--YYKKKGKLVEIDGSGDID 192
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
686-878 |
1.81e-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: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 765
Cdd:COG0563 45 LGKKAKEYMDAGELVPDEIVIGLVKERLAQPDCANGFILDGFPRTVAQAEALDELLAELGIKL----------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 766 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNLR---DQ---IQHRIIG 839
Cdd:COG0563 108 -------------DAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVCDKCGGELVQradDNeetVRKRLEV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 145699133 840 FLDN-WPLLEqwFSEPENILIKINAEIDKESLCEKVKEIL 878
Cdd:COG0563 175 YHEQtAPLID--YYRKKGKLVEIDGEGSIEEVTADILAIL 212
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
686-795 |
4.04e-08 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 55.54 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 765
Cdd:PRK00279 45 LGKEAKSYMDAGELVPDEIVIGLVKERLAQPDCKNGFLLDGFPRTIPQAEALDEMLKELGIKL----------------- 107
|
90 100 110
....*....|....*....|....*....|
gi 145699133 766 atskeiplpspafDFVILLDVSDTSSMSRM 795
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 ... |
686-741 |
1.51e-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: 53.78 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQD-CILDGFPMTLNQAQLLEEAL 741
Cdd:TIGR01351 44 LGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENgFILDGFPRTLSQAEALDALL 100
|
|
| adk |
PRK02496 |
adenylate kinase; Provisional |
680-751 |
7.91e-06 |
|
adenylate kinase; Provisional
Pssm-ID: 179433 [Multi-domain] Cd Length: 184 Bit Score: 48.21 E-value: 7.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145699133 680 LTTRAQLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLTEV 751
Cdd:PRK02496 40 IKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQPDAANGWILDGFPRKVTQAAFLDELLQEIGQSGERV 111
|
|
| PLN02674 |
PLN02674 |
adenylate kinase |
654-741 |
1.52e-05 |
|
adenylate kinase
Pssm-ID: 178279 [Multi-domain] Cd Length: 244 Bit Score: 48.34 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 654 GETMLSANADKTPkaeevkssdsflklttraqLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQ 733
Cdd:PLN02674 63 GDMLRAAVAAKTP-------------------LGIKAKEAMDKGELVSDDLVVGIIDEAMKKPSCQKGFILDGFPRTVVQ 123
|
....*...
gi 145699133 734 AQLLEEAL 741
Cdd:PLN02674 124 AQKLDEML 131
|
|
| ADK |
pfam00406 |
Adenylate kinase; |
685-742 |
2.20e-05 |
|
Adenylate kinase;
Pssm-ID: 395329 [Multi-domain] Cd Length: 184 Bit Score: 46.92 E-value: 2.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 145699133 685 QLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALT 742
Cdd:pfam00406 40 ELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFLLDGFPRTVPQAEALEELLE 97
|
|
| PRK14526 |
PRK14526 |
adenylate kinase; Provisional |
686-741 |
3.24e-05 |
|
adenylate kinase; Provisional
Pssm-ID: 172992 [Multi-domain] Cd Length: 211 Bit Score: 47.15 E-value: 3.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 741
Cdd:PRK14526 45 LGKEIKQIVENGQLVPDSITIKIVEDKINTIKNNDNFILDGFPRNINQAKALDKFL 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-447 |
4.79e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 176 EKLERFQKLKEEQRCFDIEKQYLNRRRQNEIMAKIQAAIIQIpkpasNRTLKALEAQkMMKKKKEAEDVADEIKKFEALI 255
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL-----EAELEELEAE-LAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 256 kKDLQAKESASKTSLDTAGQTTTDLLNTYSD-DEYIKKIQKRLEEDAFAREQREKRRRKLLMDQLIAHEAQEEAYREEQL 334
Cdd:COG1196 284 -EEAQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 335 INRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQDALDREAALAKQAK-IDFEEQFLKEKRFHDQI 413
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEeLEEALAELEEEEEEEEE 442
|
250 260 270
....*....|....*....|....*....|....
gi 145699133 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 |
1.45e-03 |
|
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: 43.57 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 101 YIALQKKKKSGLTGVEMQTMQRLTNLRL--QNMKSDTFQERLRHMIPRQTDFNLMRITYRF----QEKYKHVKEDLAhlh 174
Cdd:pfam17380 233 YEKMERRKESFNLAEDVTTMTPEYTVRYngQTMTENEFLNQLLHIVQHQKAVSERQQQEKFekmeQERLRQEKEEKA--- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 175 fEKLERFQKLKEEQRCFDIEKQylnrrRQNEIMAKIQAAIIQipkpaSNRTLK--ALEAQKMMKKKKEAEDVADEIKKFE 252
Cdd:pfam17380 310 -REVERRRKLEEAEKARQAEMD-----RQAAIYAEQERMAME-----RERELEriRQEERKRELERIRQEEIAMEISRMR 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 253 ALIKKDLQAKESASKTSLDTAGQTTTDLLntysDDEYIKKIQKRLEEdafareqrekrrrkllMDQLIAH--EAQEEAYR 330
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKIL----EEERQRKIQQQKVE----------------MEQIRAEqeEARQREVR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145699133 331 --EEQLINRLMRQSQQERRIAVQLMHVRHEKEVLWQNRIFREKQHEERRLKDFQD--ALDREAALAKQAKIDFEeqflKE 406
Cdd:pfam17380 439 rlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkILEKELEERKQAMIEEE----RK 514
|
330 340
....*....|....*....|....*
gi 145699133 407 KRFHDQIAVERAQARYEKHYSVCAE 431
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAE 539
|
|
| PRK14528 |
PRK14528 |
adenylate kinase; Provisional |
686-751 |
2.20e-03 |
|
adenylate kinase; Provisional
Pssm-ID: 172994 [Multi-domain] Cd Length: 186 Bit Score: 41.15 E-value: 2.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLTEV 751
Cdd:PRK14528 46 MGIEAKRYMDAGDLVPDSVVIGIIKDRIREADCKNGFLLDGFPRTVEQADALDALLKNEGKSIDKA 111
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
687-741 |
3.33e-03 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 39.53 E-value: 3.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 145699133 687 GAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 741
Cdd:pfam13207 39 LVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVIVDGHPRIKTPAGYLPGLP 93
|
|
| PRK13808 |
PRK13808 |
adenylate kinase; Provisional |
686-741 |
6.89e-03 |
|
adenylate kinase; Provisional
Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 40.64 E-value: 6.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 145699133 686 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 741
Cdd:PRK13808 45 VGLKAKDIMASGGLVPDEVVVGIISDRIEQPDAANGFILDGFPRTVPQAEALDALL 100
|
|
| |
