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Conserved domains on  [gi|568947676|ref|XP_006540855|]
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testis-specific serine kinase substrate isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TSKS super family cl25906
Testis-specific serine kinase substrate; TSKS, testis-specific serine kinase substrate, is ...
48-601 2.02e-164

Testis-specific serine kinase substrate; TSKS, testis-specific serine kinase substrate, is expressed in the testis and is downregulated in cancerous testicular tissue, in comparison with adjacent normal tissue. TSKS expression is very low to undetectable in seminoma, teratocarcinoma, embryonal, and Leydig cell tumours, while high in testicular tissue adjacent to tumours which contain pre-malignant carcinoma in situ. Recently it has been shown in human testis to be localized to the equatorial segment of ejaculated human sperm. The finding of a TSKS family member in mature sperm suggests that this family of kinases might play a role in sperm function. TSKS is localized during spermiogenesis to the centrioles of post-meiotic spermatids, where it reaches its greatest concentration during the period of flagellogenesis.


The actual alignment was detected with superfamily member pfam15358:

Pssm-ID: 434661  Cd Length: 455  Bit Score: 476.89  E-value: 2.02e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   48 KKKKAVSFHGVEPRMSHEPMHWCLNLKRSSACTNVSLLNLAAVEP-DSSGTDSTTEDSGPLALPGPPASPTTPWAPEDPD 126
Cdd:pfam15358   1 KKKKAVSFHGVEPHLASEPSKWCLNLKRSSACTNVSLLNLTDGEPdDSTTENESTDDGSPPSAPLPPIKPVPSEYDDDDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  127 ITELLSGVNSGlvrakdsitslkekttrvnqhvqtlqsecsvlsenlerrrqEAEELEGycsqlkencrkvtrsvedaei 206
Cdd:pfam15358  81 TSSQQEVSNSG-----------------------------------------EAEELEG--------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  207 ktnvlkqnsalleekLRYLQQQLQDETPRRQEAELQELEQKLEAGLSRHGLSPATPIQGCSGP--PGSPEEPPRQRGLSS 284
Cdd:pfam15358  99 ---------------LRFLQRQVQVEDLSRQGREWQELEQRMASGISKQALRPSNSEEGELPPpgAAIASINNLRRALEN 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  285 SGWGMAVRTGEGPSLSEQELQKVSTGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSA 364
Cdd:pfam15358 164 GHMGLGDEVSIDGKSNTAETQKVIAGLEELRREVSSLTARWQQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  365 RGLQELRGRADELCTMVERSAVSVASLRSELEALGPVKPILEELGRQLQNSRRGADHVLNLDRSAQGPCARCASQGQQLS 444
Cdd:pfam15358 244 RGLQELRGRADELCTMVERSAVSVASLRADLEGLGPVKPLLEELGRQLSSLRRGSELSMPLDRPERGSCARCSSQGQQLS 323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  445 TESLQQLLERALTPLVDEVKQKGLAPACPSCQRLHKKILPSPVSPaaptlLSPGAGAPGLGQTRQgrgpelhpsvgprrg 524
Cdd:pfam15358 324 TESLQQLLERALTPLVDEVKQRGLAPACPSCQRLHKKILELERQA-----LAKHVRAEALSSTLR--------------- 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  525 rsgqeptaDGQDEAgVRTE----AEGMGGGEKVATLDYMHLKMCSLHDQLSHLPLEGSTGAMGGGSNGGAPPKRGSPGSE 600
Cdd:pfam15358 384 --------LAQDEA-LRAKnlllTDKMKPEEKVASLDYLHLKMCSLHDQLSLLPLEGSPQSPGGGSAGGAPPKRGGPCPE 454

                  .
gi 568947676  601 Q 601
Cdd:pfam15358 455 Q 455
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
142-249 4.15e-07

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


The actual alignment was detected with superfamily member pfam13851:

Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 50.68  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEEL----EGYcSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:pfam13851  32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELrkqlENY-EKDKQSLKNLKARLKVLEKELKDLKWEHEV 110
                          90       100       110
                  ....*....|....*....|....*....|..
gi 568947676  218 LEEKLRYLQQQLqDETPRRQEAELQELEQKLE 249
Cdd:pfam13851 111 LEQRFEKVERER-DELYDKFEAAIQDVQQKTG 141
 
Name Accession Description Interval E-value
TSKS pfam15358
Testis-specific serine kinase substrate; TSKS, testis-specific serine kinase substrate, is ...
48-601 2.02e-164

Testis-specific serine kinase substrate; TSKS, testis-specific serine kinase substrate, is expressed in the testis and is downregulated in cancerous testicular tissue, in comparison with adjacent normal tissue. TSKS expression is very low to undetectable in seminoma, teratocarcinoma, embryonal, and Leydig cell tumours, while high in testicular tissue adjacent to tumours which contain pre-malignant carcinoma in situ. Recently it has been shown in human testis to be localized to the equatorial segment of ejaculated human sperm. The finding of a TSKS family member in mature sperm suggests that this family of kinases might play a role in sperm function. TSKS is localized during spermiogenesis to the centrioles of post-meiotic spermatids, where it reaches its greatest concentration during the period of flagellogenesis.


Pssm-ID: 434661  Cd Length: 455  Bit Score: 476.89  E-value: 2.02e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   48 KKKKAVSFHGVEPRMSHEPMHWCLNLKRSSACTNVSLLNLAAVEP-DSSGTDSTTEDSGPLALPGPPASPTTPWAPEDPD 126
Cdd:pfam15358   1 KKKKAVSFHGVEPHLASEPSKWCLNLKRSSACTNVSLLNLTDGEPdDSTTENESTDDGSPPSAPLPPIKPVPSEYDDDDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  127 ITELLSGVNSGlvrakdsitslkekttrvnqhvqtlqsecsvlsenlerrrqEAEELEGycsqlkencrkvtrsvedaei 206
Cdd:pfam15358  81 TSSQQEVSNSG-----------------------------------------EAEELEG--------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  207 ktnvlkqnsalleekLRYLQQQLQDETPRRQEAELQELEQKLEAGLSRHGLSPATPIQGCSGP--PGSPEEPPRQRGLSS 284
Cdd:pfam15358  99 ---------------LRFLQRQVQVEDLSRQGREWQELEQRMASGISKQALRPSNSEEGELPPpgAAIASINNLRRALEN 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  285 SGWGMAVRTGEGPSLSEQELQKVSTGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSA 364
Cdd:pfam15358 164 GHMGLGDEVSIDGKSNTAETQKVIAGLEELRREVSSLTARWQQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  365 RGLQELRGRADELCTMVERSAVSVASLRSELEALGPVKPILEELGRQLQNSRRGADHVLNLDRSAQGPCARCASQGQQLS 444
Cdd:pfam15358 244 RGLQELRGRADELCTMVERSAVSVASLRADLEGLGPVKPLLEELGRQLSSLRRGSELSMPLDRPERGSCARCSSQGQQLS 323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  445 TESLQQLLERALTPLVDEVKQKGLAPACPSCQRLHKKILPSPVSPaaptlLSPGAGAPGLGQTRQgrgpelhpsvgprrg 524
Cdd:pfam15358 324 TESLQQLLERALTPLVDEVKQRGLAPACPSCQRLHKKILELERQA-----LAKHVRAEALSSTLR--------------- 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  525 rsgqeptaDGQDEAgVRTE----AEGMGGGEKVATLDYMHLKMCSLHDQLSHLPLEGSTGAMGGGSNGGAPPKRGSPGSE 600
Cdd:pfam15358 384 --------LAQDEA-LRAKnlllTDKMKPEEKVASLDYLHLKMCSLHDQLSLLPLEGSPQSPGGGSAGGAPPKRGGPCPE 454

                  .
gi 568947676  601 Q 601
Cdd:pfam15358 455 Q 455
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
142-249 4.15e-07

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 50.68  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEEL----EGYcSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:pfam13851  32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELrkqlENY-EKDKQSLKNLKARLKVLEKELKDLKWEHEV 110
                          90       100       110
                  ....*....|....*....|....*....|..
gi 568947676  218 LEEKLRYLQQQLqDETPRRQEAELQELEQKLE 249
Cdd:pfam13851 111 LEQRFEKVERER-DELYDKFEAAIQDVQQKTG 141
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
143-467 4.46e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   143 DSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKEncrkvtrSVEDAEIKTNVLKQNSALLEEKL 222
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   223 RYLQQQLQ--DETPRRQEAELQELEQKLEaglsrhglspatpiqgcsgppgspeepprqrglsssgwgmavrtgegpsLS 300
Cdd:TIGR02168  305 QILRERLAnlERQLEELEAQLEELESKLD-------------------------------------------------EL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   301 EQELQKVSTGLEELRREVSSLAARWHQEEGAVQEAlrllgglGGRLDGFLGQWERAQREQAQSARGLQELRGRADELCTM 380
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEEL-------ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   381 VERSAVSVASLRSELEALG--PVKPILEELGRQLQNSRRGADHVLNLDRSAQgpcARCASQGQQLsteslqQLLERALTP 458
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLkkLEEAELKELQAELEELEEELEELQEELERLE---EALEELREEL------EEAEQALDA 479

                   ....*....
gi 568947676   459 LVDEVKQKG 467
Cdd:TIGR02168  480 AERELAQLQ 488
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-253 5.10e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 131 LSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNV 210
Cdd:COG4372   61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568947676 211 LKQNSAL-------LEEKLRYLQQQLQDETPRRQEAELQELEQKLEAGLS 253
Cdd:COG4372  141 LQSEIAEreeelkeLEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
122-324 7.40e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 122 PEDPDITELLSGVNSGLVR---AKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVT 198
Cdd:PRK03918 214 SELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 199 RSVEDAEIKTNVLKQNSAL------LEEKLRYLQQQLQDETPRRQEAE-----LQELEQKLEAGLSRHGL-SPATPIQGc 266
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIekrlsrLEEEINGIEERIKELEEKEERLEelkkkLKELEKRLEELEERHELyEEAKAKKE- 372
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947676 267 sgppgspeeppRQRGLSSSgwgmavRTGEGPSLSEQELQKVSTGLEELRREVSSLAAR 324
Cdd:PRK03918 373 -----------ELERLKKR------LTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
142-250 2.81e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEK 221
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568947676   222 LRYLQQQL----------------------------QDETPRRQEAELQELEQKLEA 250
Cdd:TIGR02169  767 IEELEEDLhkleealndlearlshsripeiqaelskLEEEVSRIEARLREIEQKLNR 823
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-249 5.52e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEgycsQLKEncrkvtrSVEDAEIKTNVLKQNSALLEEK 221
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKE-------EIEELEKELESLEGSKRKLEEK 260
                         90       100
                 ....*....|....*....|....*...
gi 568947676 222 LRYLQQQLqdetpRRQEAELQELEQKLE 249
Cdd:PRK03918 261 IRELEERI-----EELKKEIEELEEKVK 283
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
168-249 9.49e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 38.33  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 168 VLSENLERRRQEAEELEgycsQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEKLRYLQQQLQDETpRRQEAELQELEQK 247
Cdd:cd16269  171 VLQEFLQSKEAEAEAIL----QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQE-RSYEEHLRQLKEK 245

                 ..
gi 568947676 248 LE 249
Cdd:cd16269  246 ME 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
138-429 9.68e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 9.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 138 LVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:COG1196  276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 218 LEEKLRYLQQQLQDETpRRQEAELQELEQKLEAGLSRhglspatpiqgcsgppgspeepprqrglsssgwgmavrtgegp 297
Cdd:COG1196  356 AEAELAEAEEALLEAE-AELAEAEEELEELAEELLEA------------------------------------------- 391
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 298 slsEQELQKVSTGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQELRGRADEL 377
Cdd:COG1196  392 ---LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568947676 378 CTMVERSAVSVASLRSELEALGPVKPILEELGRQLQNSRRGADHVLNLDRSA 429
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
 
Name Accession Description Interval E-value
TSKS pfam15358
Testis-specific serine kinase substrate; TSKS, testis-specific serine kinase substrate, is ...
48-601 2.02e-164

Testis-specific serine kinase substrate; TSKS, testis-specific serine kinase substrate, is expressed in the testis and is downregulated in cancerous testicular tissue, in comparison with adjacent normal tissue. TSKS expression is very low to undetectable in seminoma, teratocarcinoma, embryonal, and Leydig cell tumours, while high in testicular tissue adjacent to tumours which contain pre-malignant carcinoma in situ. Recently it has been shown in human testis to be localized to the equatorial segment of ejaculated human sperm. The finding of a TSKS family member in mature sperm suggests that this family of kinases might play a role in sperm function. TSKS is localized during spermiogenesis to the centrioles of post-meiotic spermatids, where it reaches its greatest concentration during the period of flagellogenesis.


Pssm-ID: 434661  Cd Length: 455  Bit Score: 476.89  E-value: 2.02e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   48 KKKKAVSFHGVEPRMSHEPMHWCLNLKRSSACTNVSLLNLAAVEP-DSSGTDSTTEDSGPLALPGPPASPTTPWAPEDPD 126
Cdd:pfam15358   1 KKKKAVSFHGVEPHLASEPSKWCLNLKRSSACTNVSLLNLTDGEPdDSTTENESTDDGSPPSAPLPPIKPVPSEYDDDDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  127 ITELLSGVNSGlvrakdsitslkekttrvnqhvqtlqsecsvlsenlerrrqEAEELEGycsqlkencrkvtrsvedaei 206
Cdd:pfam15358  81 TSSQQEVSNSG-----------------------------------------EAEELEG--------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  207 ktnvlkqnsalleekLRYLQQQLQDETPRRQEAELQELEQKLEAGLSRHGLSPATPIQGCSGP--PGSPEEPPRQRGLSS 284
Cdd:pfam15358  99 ---------------LRFLQRQVQVEDLSRQGREWQELEQRMASGISKQALRPSNSEEGELPPpgAAIASINNLRRALEN 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  285 SGWGMAVRTGEGPSLSEQELQKVSTGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSA 364
Cdd:pfam15358 164 GHMGLGDEVSIDGKSNTAETQKVIAGLEELRREVSSLTARWQQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  365 RGLQELRGRADELCTMVERSAVSVASLRSELEALGPVKPILEELGRQLQNSRRGADHVLNLDRSAQGPCARCASQGQQLS 444
Cdd:pfam15358 244 RGLQELRGRADELCTMVERSAVSVASLRADLEGLGPVKPLLEELGRQLSSLRRGSELSMPLDRPERGSCARCSSQGQQLS 323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  445 TESLQQLLERALTPLVDEVKQKGLAPACPSCQRLHKKILPSPVSPaaptlLSPGAGAPGLGQTRQgrgpelhpsvgprrg 524
Cdd:pfam15358 324 TESLQQLLERALTPLVDEVKQRGLAPACPSCQRLHKKILELERQA-----LAKHVRAEALSSTLR--------------- 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  525 rsgqeptaDGQDEAgVRTE----AEGMGGGEKVATLDYMHLKMCSLHDQLSHLPLEGSTGAMGGGSNGGAPPKRGSPGSE 600
Cdd:pfam15358 384 --------LAQDEA-LRAKnlllTDKMKPEEKVASLDYLHLKMCSLHDQLSLLPLEGSPQSPGGGSAGGAPPKRGGPCPE 454

                  .
gi 568947676  601 Q 601
Cdd:pfam15358 455 Q 455
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
142-249 4.15e-07

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 50.68  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEEL----EGYcSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:pfam13851  32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELrkqlENY-EKDKQSLKNLKARLKVLEKELKDLKWEHEV 110
                          90       100       110
                  ....*....|....*....|....*....|..
gi 568947676  218 LEEKLRYLQQQLqDETPRRQEAELQELEQKLE 249
Cdd:pfam13851 111 LEQRFEKVERER-DELYDKFEAAIQDVQQKTG 141
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
143-467 4.46e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   143 DSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKEncrkvtrSVEDAEIKTNVLKQNSALLEEKL 222
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   223 RYLQQQLQ--DETPRRQEAELQELEQKLEaglsrhglspatpiqgcsgppgspeepprqrglsssgwgmavrtgegpsLS 300
Cdd:TIGR02168  305 QILRERLAnlERQLEELEAQLEELESKLD-------------------------------------------------EL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   301 EQELQKVSTGLEELRREVSSLAARWHQEEGAVQEAlrllgglGGRLDGFLGQWERAQREQAQSARGLQELRGRADELCTM 380
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEEL-------ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   381 VERSAVSVASLRSELEALG--PVKPILEELGRQLQNSRRGADHVLNLDRSAQgpcARCASQGQQLsteslqQLLERALTP 458
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLkkLEEAELKELQAELEELEEELEELQEELERLE---EALEELREEL------EEAEQALDA 479

                   ....*....
gi 568947676   459 LVDEVKQKG 467
Cdd:TIGR02168  480 AERELAQLQ 488
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-253 5.10e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 131 LSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNV 210
Cdd:COG4372   61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568947676 211 LKQNSAL-------LEEKLRYLQQQLQDETPRRQEAELQELEQKLEAGLS 253
Cdd:COG4372  141 LQSEIAEreeelkeLEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-249 6.02e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 131 LSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNV 210
Cdd:COG4372   75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568947676 211 LKQNSALLEEKLRYLQQQLQDETPRRQEAELQELEQKLE 249
Cdd:COG4372  155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
122-324 7.40e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 122 PEDPDITELLSGVNSGLVR---AKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVT 198
Cdd:PRK03918 214 SELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 199 RSVEDAEIKTNVLKQNSAL------LEEKLRYLQQQLQDETPRRQEAE-----LQELEQKLEAGLSRHGL-SPATPIQGc 266
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIekrlsrLEEEINGIEERIKELEEKEERLEelkkkLKELEKRLEELEERHELyEEAKAKKE- 372
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947676 267 sgppgspeeppRQRGLSSSgwgmavRTGEGPSLSEQELQKVSTGLEELRREVSSLAAR 324
Cdd:PRK03918 373 -----------ELERLKKR------LTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
126-383 1.28e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   126 DITELLSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKEncrkvtrSVEDAE 205
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA-------ELEELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   206 IKTNVLKQNSALLEEKLRYLQQQLQD--ETPRRQEAELQELEQKLEAglsrhglspatpiqgcsgppgspeEPPRQRGLS 283
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQleLQIASLNNEIERLEARLER------------------------LEDRRERLQ 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   284 SSgwgmavRTGEGPSLSEQELQKVSTGLEELRREVSSLAARWHQEEGAVQEAlrllgglggrldgfLGQWERAQREQAQS 363
Cdd:TIGR02168  421 QE------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL--------------REELEEAEQALDAA 480
                          250       260
                   ....*....|....*....|
gi 568947676   364 ARGLQELRGRADELCTMVER 383
Cdd:TIGR02168  481 ERELAQLQARLDSLERLQEN 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
142-250 2.81e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEK 221
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568947676   222 LRYLQQQL----------------------------QDETPRRQEAELQELEQKLEA 250
Cdd:TIGR02169  767 IEELEEDLhkleealndlearlshsripeiqaelskLEEEVSRIEARLREIEQKLNR 823
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
168-254 6.42e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 41.55  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  168 VLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEKLRYLQQQLQDETPRRQEAElqELEQK 247
Cdd:pfam00261 124 VVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAE--RSVQK 201

                  ....*..
gi 568947676  248 LEAGLSR 254
Cdd:pfam00261 202 LEKEVDR 208
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
138-401 1.81e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   138 LVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   218 LEEKLRYLQQQLQdetprRQEAELQELEQ---KLEAGLSRHGLSPATPIQGCSGPPGSPEEPPRQRGLSSSGWgmAVRTG 294
Cdd:TIGR02168  780 AEAEIEELEAQIE-----QLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSE 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   295 EGPSLS------EQELQKVSTGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQ 368
Cdd:TIGR02168  853 DIESLAaeieelEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568947676   369 ELRGRADELCTMV----------------------ERSAVSVASLRSELEALGPV 401
Cdd:TIGR02168  933 GLEVRIDNLQERLseeysltleeaealenkieddeEEARRRLKRLENKIKELGPV 987
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
125-253 2.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 125 PDITELLSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDA 204
Cdd:COG4372   20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568947676 205 EIKTNVLKQNSALLEEKLRYLQQQLQDEtpRRQEAELQELEQKLEAGLS 253
Cdd:COG4372  100 QEELESLQEEAEELQEELEELQKERQDL--EQQRKQLEAQIAELQSEIA 146
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
290-407 2.92e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   290 AVRTGEGPSLSE-QELQKVSTGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQ 368
Cdd:TIGR02169  661 APRGGILFSRSEpAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568947676   369 ELRGRADELctmversAVSVASLRSELEALGPVKPILEE 407
Cdd:TIGR02169  741 ELEEDLSSL-------EQEIENVKSELKELEARIEELEE 772
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
142-250 4.90e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.81  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676  142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEK 221
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
                          90       100
                  ....*....|....*....|....*....
gi 568947676  222 LRYLQQQLQDETprRQEAELQELEQKLEA 250
Cdd:pfam10174 403 IENLQEQLRDKD--KQLAGLKERVKSLQT 429
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-249 5.52e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEgycsQLKEncrkvtrSVEDAEIKTNVLKQNSALLEEK 221
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKE-------EIEELEKELESLEGSKRKLEEK 260
                         90       100
                 ....*....|....*....|....*...
gi 568947676 222 LRYLQQQLqdetpRRQEAELQELEQKLE 249
Cdd:PRK03918 261 IRELEERI-----EELKKEIEELEEKVK 283
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-455 6.57e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   301 EQELQKVSTGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQELRGRADELCTM 380
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676   381 VERSAVSVASLRSEL----EALGPVKPILEELGRQLQNSRRGADHVLNLDRSAQGPCARCASQGQQLS--TESLQQLLER 454
Cdd:TIGR02168  777 LAEAEAEIEELEAQIeqlkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqIEELSEDIES 856

                   .
gi 568947676   455 A 455
Cdd:TIGR02168  857 L 857
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
168-249 9.49e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 38.33  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 168 VLSENLERRRQEAEELEgycsQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEKLRYLQQQLQDETpRRQEAELQELEQK 247
Cdd:cd16269  171 VLQEFLQSKEAEAEAIL----QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQE-RSYEEHLRQLKEK 245

                 ..
gi 568947676 248 LE 249
Cdd:cd16269  246 ME 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
138-429 9.68e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 9.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 138 LVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:COG1196  276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 218 LEEKLRYLQQQLQDETpRRQEAELQELEQKLEAGLSRhglspatpiqgcsgppgspeepprqrglsssgwgmavrtgegp 297
Cdd:COG1196  356 AEAELAEAEEALLEAE-AELAEAEEELEELAEELLEA------------------------------------------- 391
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947676 298 slsEQELQKVSTGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQELRGRADEL 377
Cdd:COG1196  392 ---LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568947676 378 CTMVERSAVSVASLRSELEALGPVKPILEELGRQLQNSRRGADHVLNLDRSA 429
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
 
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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