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Conserved domains on  [gi|564327991|ref|XP_006229079|]
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testis-specific serine kinase substrate isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TSKS pfam15358
Testis-specific serine kinase substrate; TSKS, testis-specific serine kinase substrate, is ...
48-576 0e+00

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: 580.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   48 KKKKAVSFHGVEPRMSHEPMHWCLNLKRSSACTNVSLLNLAAMEP-DSSGTDSTTEDSGPLALPGPPASPTTPWAPEDPD 126
Cdd:pfam15358   1 KKKKAVSFHGVEPHLASEPSKWCLNLKRSSACTNVSLLNLTDGEPdDSTTENESTDDGSPPSAPLPPIKPVPSEYDDDDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  127 ITELLSGVNSGlvrakdsitslkekttrvnqhvqtlqsecsvlsenlerrrqEAEELEGycsqlkencrkvtrsvedaei 206
Cdd:pfam15358  81 TSSQQEVSNSG-----------------------------------------EAEELEG--------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  207 ktnvlkqnsalleekLRYLQQQLQDETPRRQEAELQELEQKLEAGLSRHGLGPTTPIQGCSGP--PGSPEEPPRPRGLPS 284
Cdd:pfam15358  99 ---------------LRFLQRQVQVEDLSRQGREWQELEQRMASGISKQALRPSNSEEGELPPpgAAIASINNLRRALEN 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  285 NGWGMAIRAGEGPSLSEQELQKVSSGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSA 364
Cdd:pfam15358 164 GHMGLGDEVSIDGKSNTAETQKVIAGLEELRREVSSLTARWQQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  365 RGLQELRGRADELCTMVERSAVSVASLRSELEALGPVKPILEELGRQLQNSRRGPDHVLNLDRPAQGPCPRCASQGQQLS 444
Cdd:pfam15358 244 RGLQELRGRADELCTMVERSAVSVASLRADLEGLGPVKPLLEELGRQLSSLRRGSELSMPLDRPERGSCARCSSQGQQLS 323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  445 TESLQQLLERALTPLVDEVKQKGLAPACPSCQRLHKKILELERQALAKHVRAEALSSTLRLAQDEAVRAKNLLLTDKMKP 524
Cdd:pfam15358 324 TESLQQLLERALTPLVDEVKQRGLAPACPSCQRLHKKILELERQALAKHVRAEALSSTLRLAQDEALRAKNLLLTDKMKP 403
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564327991  525 EEKVATLDYMHLKMCSLHDQLSHLPLEGSTGAMGGGSTGGAPPKRGGPGSEQ 576
Cdd:pfam15358 404 EEKVASLDYLHLKMCSLHDQLSLLPLEGSPQSPGGGSAGGAPPKRGGPCPEQ 455
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
142-249 5.06e-06

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: 47.59  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEEL----EGYcSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:pfam13851  32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELrkqlENY-EKDKQSLKNLKARLKVLEKELKDLKWEHEV 110
                          90       100       110
                  ....*....|....*....|....*....|..
gi 564327991  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 ...
48-576 0e+00

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: 580.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   48 KKKKAVSFHGVEPRMSHEPMHWCLNLKRSSACTNVSLLNLAAMEP-DSSGTDSTTEDSGPLALPGPPASPTTPWAPEDPD 126
Cdd:pfam15358   1 KKKKAVSFHGVEPHLASEPSKWCLNLKRSSACTNVSLLNLTDGEPdDSTTENESTDDGSPPSAPLPPIKPVPSEYDDDDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  127 ITELLSGVNSGlvrakdsitslkekttrvnqhvqtlqsecsvlsenlerrrqEAEELEGycsqlkencrkvtrsvedaei 206
Cdd:pfam15358  81 TSSQQEVSNSG-----------------------------------------EAEELEG--------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  207 ktnvlkqnsalleekLRYLQQQLQDETPRRQEAELQELEQKLEAGLSRHGLGPTTPIQGCSGP--PGSPEEPPRPRGLPS 284
Cdd:pfam15358  99 ---------------LRFLQRQVQVEDLSRQGREWQELEQRMASGISKQALRPSNSEEGELPPpgAAIASINNLRRALEN 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  285 NGWGMAIRAGEGPSLSEQELQKVSSGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSA 364
Cdd:pfam15358 164 GHMGLGDEVSIDGKSNTAETQKVIAGLEELRREVSSLTARWQQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  365 RGLQELRGRADELCTMVERSAVSVASLRSELEALGPVKPILEELGRQLQNSRRGPDHVLNLDRPAQGPCPRCASQGQQLS 444
Cdd:pfam15358 244 RGLQELRGRADELCTMVERSAVSVASLRADLEGLGPVKPLLEELGRQLSSLRRGSELSMPLDRPERGSCARCSSQGQQLS 323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  445 TESLQQLLERALTPLVDEVKQKGLAPACPSCQRLHKKILELERQALAKHVRAEALSSTLRLAQDEAVRAKNLLLTDKMKP 524
Cdd:pfam15358 324 TESLQQLLERALTPLVDEVKQRGLAPACPSCQRLHKKILELERQALAKHVRAEALSSTLRLAQDEALRAKNLLLTDKMKP 403
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564327991  525 EEKVATLDYMHLKMCSLHDQLSHLPLEGSTGAMGGGSTGGAPPKRGGPGSEQ 576
Cdd:pfam15358 404 EEKVASLDYLHLKMCSLHDQLSLLPLEGSPQSPGGGSAGGAPPKRGGPCPEQ 455
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
142-249 5.06e-06

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: 47.59  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEEL----EGYcSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:pfam13851  32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELrkqlENY-EKDKQSLKNLKARLKVLEKELKDLKWEHEV 110
                          90       100       110
                  ....*....|....*....|....*....|..
gi 564327991  218 LEEKLRYLQQQLqDETPRRQEAELQELEQKLE 249
Cdd:pfam13851 111 LEQRFEKVERER-DELYDKFEAAIQDVQQKTG 141
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
143-412 3.37e-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: 43.89  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   143 DSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKEncrkvtrSVEDAEIKTNVLKQNSALLEEKL 222
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   223 RYLQQQLQ--DETPRRQEAELQELEQKLEaglsrhglgpttpiqgcsgppgspeepprprglpsngwgmairagegpsLS 300
Cdd:TIGR02168  305 QILRERLAnlERQLEELEAQLEELESKLD-------------------------------------------------EL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   301 EQELQKVSSGLEELRREVSSLAARwhqeegaVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQELRGRADELCTM 380
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAE-------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270
                   ....*....|....*....|....*....|....
gi 564327991   381 VERSAVSVASLRSELEALG--PVKPILEELGRQL 412
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLkkLEEAELKELQAEL 442
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-249 4.11e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 131 LSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNV 210
Cdd:COG4372   75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564327991 211 LKQNSALLEEKLRYLQQQLQDETPRRQEAELQELEQKLE 249
Cdd:COG4372  155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
142-250 7.39e-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: 42.75  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEK 221
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564327991   222 LRYLQQQL----------------------------QDETPRRQEAELQELEQKLEA 250
Cdd:TIGR02169  767 IEELEEDLhkleealndlearlshsripeiqaelskLEEEVSRIEARLREIEQKLNR 823
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
122-249 7.61e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 122 PEDPDITELLSGVNSGLVR---AKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVT 198
Cdd:PRK03918 214 SELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564327991 199 RSVEDAEIKTNVLKQNSAL------LEEKLRYLQQQLQDETprRQEAELQELEQKLE 249
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIekrlsrLEEEINGIEERIKELE--EKEERLEELKKKLK 348
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
140-409 2.16e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 140 RAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLE 219
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 220 EKLRYLQQQLQDETPRRQEAE--LQELEQKLEAGLSrhglgPTtpiqgCsgppgspeepprprGLPSNGWGMAIRAGEgp 297
Cdd:PRK02224 419 EERDELREREAELEATLRTARerVEEAEALLEAGKC-----PE-----C--------------GQPVEGSPHVETIEE-- 472
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 298 slSEQELQKVSSGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARgLQELRGRADEL 377
Cdd:PRK02224 473 --DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAEL 549
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564327991 378 CTMVE--RSAVSVASLRSElEALGPVKPILEELG 409
Cdd:PRK02224 550 EAEAEekREAAAEAEEEAE-EAREEVAELNSKLA 582
 
Name Accession Description Interval E-value
TSKS pfam15358
Testis-specific serine kinase substrate; TSKS, testis-specific serine kinase substrate, is ...
48-576 0e+00

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: 580.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   48 KKKKAVSFHGVEPRMSHEPMHWCLNLKRSSACTNVSLLNLAAMEP-DSSGTDSTTEDSGPLALPGPPASPTTPWAPEDPD 126
Cdd:pfam15358   1 KKKKAVSFHGVEPHLASEPSKWCLNLKRSSACTNVSLLNLTDGEPdDSTTENESTDDGSPPSAPLPPIKPVPSEYDDDDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  127 ITELLSGVNSGlvrakdsitslkekttrvnqhvqtlqsecsvlsenlerrrqEAEELEGycsqlkencrkvtrsvedaei 206
Cdd:pfam15358  81 TSSQQEVSNSG-----------------------------------------EAEELEG--------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  207 ktnvlkqnsalleekLRYLQQQLQDETPRRQEAELQELEQKLEAGLSRHGLGPTTPIQGCSGP--PGSPEEPPRPRGLPS 284
Cdd:pfam15358  99 ---------------LRFLQRQVQVEDLSRQGREWQELEQRMASGISKQALRPSNSEEGELPPpgAAIASINNLRRALEN 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  285 NGWGMAIRAGEGPSLSEQELQKVSSGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSA 364
Cdd:pfam15358 164 GHMGLGDEVSIDGKSNTAETQKVIAGLEELRREVSSLTARWQQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  365 RGLQELRGRADELCTMVERSAVSVASLRSELEALGPVKPILEELGRQLQNSRRGPDHVLNLDRPAQGPCPRCASQGQQLS 444
Cdd:pfam15358 244 RGLQELRGRADELCTMVERSAVSVASLRADLEGLGPVKPLLEELGRQLSSLRRGSELSMPLDRPERGSCARCSSQGQQLS 323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  445 TESLQQLLERALTPLVDEVKQKGLAPACPSCQRLHKKILELERQALAKHVRAEALSSTLRLAQDEAVRAKNLLLTDKMKP 524
Cdd:pfam15358 324 TESLQQLLERALTPLVDEVKQRGLAPACPSCQRLHKKILELERQALAKHVRAEALSSTLRLAQDEALRAKNLLLTDKMKP 403
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564327991  525 EEKVATLDYMHLKMCSLHDQLSHLPLEGSTGAMGGGSTGGAPPKRGGPGSEQ 576
Cdd:pfam15358 404 EEKVASLDYLHLKMCSLHDQLSLLPLEGSPQSPGGGSAGGAPPKRGGPCPEQ 455
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
142-249 5.06e-06

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: 47.59  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEEL----EGYcSQLKENCRKVTRSVEDAEIKTNVLKQNSAL 217
Cdd:pfam13851  32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELrkqlENY-EKDKQSLKNLKARLKVLEKELKDLKWEHEV 110
                          90       100       110
                  ....*....|....*....|....*....|..
gi 564327991  218 LEEKLRYLQQQLqDETPRRQEAELQELEQKLE 249
Cdd:pfam13851 111 LEQRFEKVERER-DELYDKFEAAIQDVQQKTG 141
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
143-412 3.37e-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: 43.89  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   143 DSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKEncrkvtrSVEDAEIKTNVLKQNSALLEEKL 222
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   223 RYLQQQLQ--DETPRRQEAELQELEQKLEaglsrhglgpttpiqgcsgppgspeepprprglpsngwgmairagegpsLS 300
Cdd:TIGR02168  305 QILRERLAnlERQLEELEAQLEELESKLD-------------------------------------------------EL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   301 EQELQKVSSGLEELRREVSSLAARwhqeegaVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQELRGRADELCTM 380
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAE-------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
                          250       260       270
                   ....*....|....*....|....*....|....
gi 564327991   381 VERSAVSVASLRSELEALG--PVKPILEELGRQL 412
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLkkLEEAELKELQAEL 442
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-249 4.11e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 131 LSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNV 210
Cdd:COG4372   75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564327991 211 LKQNSALLEEKLRYLQQQLQDETPRRQEAELQELEQKLE 249
Cdd:COG4372  155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-253 4.81e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 131 LSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNV 210
Cdd:COG4372   61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 564327991 211 LKQNSAL-------LEEKLRYLQQQLQDETPRRQEAELQELEQKLEAGLS 253
Cdd:COG4372  141 LQSEIAEreeelkeLEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
142-250 7.39e-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: 42.75  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   142 KDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEK 221
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564327991   222 LRYLQQQL----------------------------QDETPRRQEAELQELEQKLEA 250
Cdd:TIGR02169  767 IEELEEDLhkleealndlearlshsripeiqaelskLEEEVSRIEARLREIEQKLNR 823
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
122-249 7.61e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 122 PEDPDITELLSGVNSGLVR---AKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVT 198
Cdd:PRK03918 214 SELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564327991 199 RSVEDAEIKTNVLKQNSAL------LEEKLRYLQQQLQDETprRQEAELQELEQKLE 249
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIekrlsrLEEEINGIEERIKELE--EKEERLEELKKKLK 348
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
126-383 1.08e-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: 41.97  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   126 DITELLSGVNSGLVRAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKEncrkvtrSVEDAE 205
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA-------ELEELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   206 IKTNVLKQNSALLEEKLRYL---------QQQLQDETPRRQEAELQELEQKLEAGLSRhglgpttpiqgcsgppgspeep 276
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLrskvaqlelQIASLNNEIERLEARLERLEDRRERLQQE---------------------- 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   277 prprglpsngwgmaiRAGEGPSLSEQELQKVSSGLEELRREVSSLAARWHQEEGAVQEAlrllgglggrldgfLGQWERA 356
Cdd:TIGR02168  423 ---------------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL--------------REELEEA 473
                          250       260
                   ....*....|....*....|....*..
gi 564327991   357 QREQAQSARGLQELRGRADELCTMVER 383
Cdd:TIGR02168  474 EQALDAAERELAQLQARLDSLERLQEN 500
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
140-409 2.16e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 140 RAKDSITSLKEKTTRVNQHVQTLQSECSVLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLE 219
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 220 EKLRYLQQQLQDETPRRQEAE--LQELEQKLEAGLSrhglgPTtpiqgCsgppgspeepprprGLPSNGWGMAIRAGEgp 297
Cdd:PRK02224 419 EERDELREREAELEATLRTARerVEEAEALLEAGKC-----PE-----C--------------GQPVEGSPHVETIEE-- 472
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991 298 slSEQELQKVSSGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARgLQELRGRADEL 377
Cdd:PRK02224 473 --DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAEL 549
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564327991 378 CTMVE--RSAVSVASLRSElEALGPVKPILEELG 409
Cdd:PRK02224 550 EAEAEekREAAAEAEEEAE-EAREEVAELNSKLA 582
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
168-254 2.52e-03

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: 39.63  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991  168 VLSENLERRRQEAEELEGYCSQLKENCRKVTRSVEDAEIKTNVLKQNSALLEEKLRYLQQQLQDETPRRQEAElqELEQK 247
Cdd:pfam00261 124 VVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAE--RSVQK 201

                  ....*..
gi 564327991  248 LEAGLSR 254
Cdd:pfam00261 202 LEKEVDR 208
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
290-407 4.56e-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: 40.05  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   290 AIRAGEGPSLSE-QELQKVSSGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQ 368
Cdd:TIGR02169  661 APRGGILFSRSEpAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 564327991   369 ELRGRADELctmversAVSVASLRSELEALGPVKPILEE 407
Cdd:TIGR02169  741 ELEEDLSSL-------EQEIENVKSELKELEARIEELEE 772
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-532 6.20e-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: 6.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   301 EQELQKVSSGLEELRREVSSLAARWHQEEGAVQEALRLLGGLGGRLDGFLGQWERAQREQAQSARGLQELRGRADELCTM 380
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327991   381 VERSAVSVASLRSELEALgpvKPILEELGRQLQNSRRGP----DHVLNL-DRPAQGPCPRCASQGQQLSTESLQQLLERA 455
Cdd:TIGR02168  339 LAELEEKLEELKEELESL---EAELEELEAELEELESRLeeleEQLETLrSKVAQLELQIASLNNEIERLEARLERLEDR 415
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564327991   456 LTPLVDEVKQKGLAPACPSCQRLHKKILELERQALAKHVRAEALSSTLRLAQDEAVRAKNLLLTDKMKPEEKVATLD 532
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
 
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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