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Conserved domains on  [gi|1720400152|ref|XP_030107795|]
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hamartin isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Hamartin pfam04388
Hamartin protein; This family includes the hamartin protein which is thought to function as a ...
7-715 0e+00

Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.


:

Pssm-ID: 461287 [Multi-domain]  Cd Length: 730  Bit Score: 994.57  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152    7 IGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATR 86
Cdd:pfam04388    1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152   87 LSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388   81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  167 KKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388  161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  247 WKTLETHDVVIECAKISLDPTEASYEDGYSVShqlsacfpyrSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQL 326
Cdd:pfam04388  241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  327 PQSLSSPSTRLLPEPLqaSLWSPSAVCGMTTPPTSPGNVPA-------DLSHPYSKAFGTTG--GKGTPSG--TPATSPP 395
Cdd:pfam04388  311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPTtpselspSSSHLSSRGSSPPEaaGEATPETtpAKDSPYL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  396 PAPPCPQDDCVHGS--AAQASATAPRKEERADSSRPYLHRQ----SNDRGLEDPPGSKGSVTLRNLPDFLGDLA-SEEDS 468
Cdd:pfam04388  389 KQPPPLSDSHVHRAlpASSQPSSPPRKDGRSQSSFPPLSKQaptnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  469 IEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYR--DSLSGSQRK--------THSAASGTQGSSVNPE-----PLH 533
Cdd:pfam04388  469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  534 SSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTAC 613
Cdd:pfam04388  549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  614 HFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFGGSPPSDELRTLRDQLLL 693
Cdd:pfam04388  629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGGSAPSDELTTLRDQLLL 708
                          730       740
                   ....*....|....*....|..
gi 1720400152  694 LHNQLLYERFKRQQHALRNRRL 715
Cdd:pfam04388  709 LHNQLLYERYKREQHAERNRRL 730
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
700-946 3.62e-10

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.69  E-value: 3.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  700 YERFKRQQHALrNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQ 779
Cdd:TIGR02168  290 LYALANEISRL-EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  780 HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLV--------- 850
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqae 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  851 LGEVNELyLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHlLLEQKKYLEDVK 930
Cdd:TIGR02168  442 LEELEEE-LEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQ 515
                          250       260
                   ....*....|....*....|..
gi 1720400152  931 SQASG------QLLAAESRYEA 946
Cdd:TIGR02168  516 SGLSGilgvlsELISVDEGYEA 537
 
Name Accession Description Interval E-value
Hamartin pfam04388
Hamartin protein; This family includes the hamartin protein which is thought to function as a ...
7-715 0e+00

Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.


Pssm-ID: 461287 [Multi-domain]  Cd Length: 730  Bit Score: 994.57  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152    7 IGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATR 86
Cdd:pfam04388    1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152   87 LSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388   81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  167 KKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388  161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  247 WKTLETHDVVIECAKISLDPTEASYEDGYSVShqlsacfpyrSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQL 326
Cdd:pfam04388  241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  327 PQSLSSPSTRLLPEPLqaSLWSPSAVCGMTTPPTSPGNVPA-------DLSHPYSKAFGTTG--GKGTPSG--TPATSPP 395
Cdd:pfam04388  311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPTtpselspSSSHLSSRGSSPPEaaGEATPETtpAKDSPYL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  396 PAPPCPQDDCVHGS--AAQASATAPRKEERADSSRPYLHRQ----SNDRGLEDPPGSKGSVTLRNLPDFLGDLA-SEEDS 468
Cdd:pfam04388  389 KQPPPLSDSHVHRAlpASSQPSSPPRKDGRSQSSFPPLSKQaptnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  469 IEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYR--DSLSGSQRK--------THSAASGTQGSSVNPE-----PLH 533
Cdd:pfam04388  469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  534 SSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTAC 613
Cdd:pfam04388  549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  614 HFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFGGSPPSDELRTLRDQLLL 693
Cdd:pfam04388  629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGGSAPSDELTTLRDQLLL 708
                          730       740
                   ....*....|....*....|..
gi 1720400152  694 LHNQLLYERFKRQQHALRNRRL 715
Cdd:pfam04388  709 LHNQLLYERYKREQHAERNRRL 730
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
700-946 3.62e-10

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: 64.69  E-value: 3.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  700 YERFKRQQHALrNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQ 779
Cdd:TIGR02168  290 LYALANEISRL-EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  780 HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLV--------- 850
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqae 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  851 LGEVNELyLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHlLLEQKKYLEDVK 930
Cdd:TIGR02168  442 LEELEEE-LEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQ 515
                          250       260
                   ....*....|....*....|..
gi 1720400152  931 SQASG------QLLAAESRYEA 946
Cdd:TIGR02168  516 SGLSGilgvlsELISVDEGYEA 537
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
752-965 1.17e-09

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 59.94  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  752 KEQARYSQLQEqRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKL 831
Cdd:COG1579      4 EDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  832 SNSESvqqqmeflNRQllvlgevnelyLEQLQskhpdttKEVEMMKTAyRKELEKnrsHLLQQNQRLDASQRRVLELESL 911
Cdd:COG1579     83 GNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAE 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720400152  912 LAKKDHLLLEQKKYLEdvksQASGQLLAAESRYEAQR-KITRVLELEILDLYGRL 965
Cdd:COG1579    133 LAELEAELEEKKAELD----EELAELEAELEELEAEReELAAKIPPELLALYERI 183
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
721-957 9.81e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.59  E-value: 9.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  721 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCR 800
Cdd:PRK02224   350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  801 NMIAELRVELKKANNKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQSKHPDT 869
Cdd:PRK02224   426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  870 TKEVEMMKTAyrKELEKNRSHLLqqnQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA-ESRYEAQR 948
Cdd:PRK02224   495 EERLERAEDL--VEAEDRIERLE---ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaEAEEEAEE 569

                   ....*....
gi 1720400152  949 KITRVLELE 957
Cdd:PRK02224   570 AREEVAELN 578
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
725-965 1.67e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 55.50  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  725 LEEHNAAMKDQLKLQEKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSqirQLQHDREEFYNQSQELQTKL----EDCR 800
Cdd:pfam05483  504 LTQEASDMTLELKKHQEDI----INCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLdkseENAR 576
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  801 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFL-------NRQLLVLG-EVNELYLEqLQSkhpdTTKE 872
Cdd:pfam05483  577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaeNKQLNAYEiKVNKLELE-LAS----AKQK 651
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  873 VEMMKTAYRKELEKNR---SHLLQQNQRLDASQRRVLELESLLAKK-DHLLLEQKKYLEDVKSQ-------ASGQLLAAE 941
Cdd:pfam05483  652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHKIAEMVALMEKHKHQydkiieeRDSELGLYK 731
                          250       260
                   ....*....|....*....|....
gi 1720400152  942 SRYEAQRKITRVLELEILDLYGRL 965
Cdd:pfam05483  732 NKEQEQSSAKAALEIELSNIKAEL 755
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
722-817 2.99e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 2.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152   722 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSqlQEQRDTMVTQLHSQIRQLQHDREEFynqSQELQTKLedcRN 801
Cdd:smart00935   20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
                            90
                    ....*....|....*.
gi 1720400152   802 MIAELRVELKKANNKV 817
Cdd:smart00935   92 ELQKILDKINKAIKEV 107
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
759-844 6.36e-03

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 39.17  E-value: 6.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  759 QLQEQRdtMVTQ-LHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELK-KANNKVCHTELLLSQVSQKLSn 833
Cdd:cd16855      9 QLEELR--QRTQeTENDLRNLQQKQESFviqYQESQKIQAQLQQLQQQPQNERIELEqQLQQQKEQLEQLLNAKAQELL- 85
                           90
                   ....*....|.
gi 1720400152  834 sesvQQQMEFL 844
Cdd:cd16855     86 ----QLRMELA 92
 
Name Accession Description Interval E-value
Hamartin pfam04388
Hamartin protein; This family includes the hamartin protein which is thought to function as a ...
7-715 0e+00

Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.


Pssm-ID: 461287 [Multi-domain]  Cd Length: 730  Bit Score: 994.57  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152    7 IGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATR 86
Cdd:pfam04388    1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152   87 LSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388   81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  167 KKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388  161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  247 WKTLETHDVVIECAKISLDPTEASYEDGYSVShqlsacfpyrSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQL 326
Cdd:pfam04388  241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  327 PQSLSSPSTRLLPEPLqaSLWSPSAVCGMTTPPTSPGNVPA-------DLSHPYSKAFGTTG--GKGTPSG--TPATSPP 395
Cdd:pfam04388  311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPTtpselspSSSHLSSRGSSPPEaaGEATPETtpAKDSPYL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  396 PAPPCPQDDCVHGS--AAQASATAPRKEERADSSRPYLHRQ----SNDRGLEDPPGSKGSVTLRNLPDFLGDLA-SEEDS 468
Cdd:pfam04388  389 KQPPPLSDSHVHRAlpASSQPSSPPRKDGRSQSSFPPLSKQaptnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  469 IEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYR--DSLSGSQRK--------THSAASGTQGSSVNPE-----PLH 533
Cdd:pfam04388  469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  534 SSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTAC 613
Cdd:pfam04388  549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  614 HFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFGGSPPSDELRTLRDQLLL 693
Cdd:pfam04388  629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGGSAPSDELTTLRDQLLL 708
                          730       740
                   ....*....|....*....|..
gi 1720400152  694 LHNQLLYERFKRQQHALRNRRL 715
Cdd:pfam04388  709 LHNQLLYERYKREQHAERNRRL 730
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
700-946 3.62e-10

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: 64.69  E-value: 3.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  700 YERFKRQQHALrNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQ 779
Cdd:TIGR02168  290 LYALANEISRL-EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  780 HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLV--------- 850
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqae 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  851 LGEVNELyLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHlLLEQKKYLEDVK 930
Cdd:TIGR02168  442 LEELEEE-LEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQ 515
                          250       260
                   ....*....|....*....|..
gi 1720400152  931 SQASG------QLLAAESRYEA 946
Cdd:TIGR02168  516 SGLSGilgvlsELISVDEGYEA 537
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
701-972 7.19e-10

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: 63.54  E-value: 7.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  701 ERFKRQQHALRNrrlLRKVIRAAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQARY-SQLQEQRDTMvTQLHSQIRQLQ 779
Cdd:TIGR02168  213 ERYKELKAELRE---LELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELeEKLEELRLEV-SELEEEIEELQ 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  780 HdreEFYNQSQELQT----------KLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLS----NSESVQQQMEFLN 845
Cdd:TIGR02168  288 K---ELYALANEISRleqqkqilreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELE 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  846 RQLLVLGEVNELY---LEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKD-HLLLE 921
Cdd:TIGR02168  365 AELEELESRLEELeeqLETLRSKVAQLELQIA----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQA 440
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720400152  922 QKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRL-EKDGRLR 972
Cdd:TIGR02168  441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaQLQARLD 492
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
752-965 1.17e-09

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 59.94  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  752 KEQARYSQLQEqRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKL 831
Cdd:COG1579      4 EDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  832 SNSESvqqqmeflNRQllvlgevnelyLEQLQskhpdttKEVEMMKTAyRKELEKnrsHLLQQNQRLDASQRRVLELESL 911
Cdd:COG1579     83 GNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAE 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720400152  912 LAKKDHLLLEQKKYLEdvksQASGQLLAAESRYEAQR-KITRVLELEILDLYGRL 965
Cdd:COG1579    133 LAELEAELEEKKAELD----EELAELEAELEELEAEReELAAKIPPELLALYERI 183
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
711-958 2.88e-09

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 61.19  E-value: 2.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  711 RNRRLLRKVIRaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL-QHDR--EEFYN 787
Cdd:TIGR04523  212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  788 QSQELQTKLEDCRN-----MIAELRVELKKANNKVCHTELLLSQVSQKLS--------------NSES----VQQQMEFL 844
Cdd:TIGR04523  289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqisqlkkeltNSESenseKQRELEEK 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  845 NRQLLVLGEVNELYLEQLQSkhpdttkeVEMMKTAYRKELEKNRshllQQNQRLDaSQRRVLELESLLAKKDHLLL---- 920
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKN--------LESQINDLESKIQNQE----KLNQQKD-EQIKKLQQEKELLEKEIERLketi 435
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1720400152  921 -EQKKYLEDVKSQASGQLLAAES---RYEAQRKITRVLELEI 958
Cdd:TIGR04523  436 iKNNSEIKDLTNQDSVKELIIKNldnTRESLETQLKVLSRSI 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
704-984 4.31e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 4.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  704 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDRE 783
Cdd:COG1196    244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  784 EFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEflnRQLLvlgEVNELYLEQLQ 863
Cdd:COG1196    320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELE---ELAEELLEALR 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  864 SKhpdttkevemmkTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESR 943
Cdd:COG1196    394 AA------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1720400152  944 YEAQRKITRVLELEILDLYGRLEKDGRLRKLEEDRAEAAEA 984
Cdd:COG1196    462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
701-957 8.87e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 8.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  701 ERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQH 780
Cdd:COG1196    213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQA 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  781 DREEFYNQSQELQTKLEDCRNMIAELRVELKKannkvchtelLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLE 860
Cdd:COG1196    289 EEYELLAELARLEQDIARLEERRRELEERLEE----------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  861 QLQskhpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA 940
Cdd:COG1196    359 ELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
                          250
                   ....*....|....*..
gi 1720400152  941 ESRYEAQRKITRVLELE 957
Cdd:COG1196    435 EEEEEEEEALEEAAEEE 451
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
709-973 3.93e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.83  E-value: 3.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  709 ALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQHDREEFYNQ 788
Cdd:COG4372     27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  789 SQELQTKLEDCRNMIAELRVE---LKKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQlqs 864
Cdd:COG4372    103 LESLQEEAEELQEELEELQKErqdLEQQRKQLEAQiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--- 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  865 khpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKK------DHLLLEQKKYLEDVKSQASGQLL 938
Cdd:COG4372    180 ---EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLeaklglALSALLDALELEEDKEELLEEVI 256
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1720400152  939 AAEsRYEAQRKITRVLELEILDLYGRLEKDGRLRK 973
Cdd:COG4372    257 LKE-IEELELAILVEKDTEEEELEIAALELEALEE 290
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
721-957 9.81e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.59  E-value: 9.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  721 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCR 800
Cdd:PRK02224   350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  801 NMIAELRVELKKANNKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQSKHPDT 869
Cdd:PRK02224   426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  870 TKEVEMMKTAyrKELEKNRSHLLqqnQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA-ESRYEAQR 948
Cdd:PRK02224   495 EERLERAEDL--VEAEDRIERLE---ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaEAEEEAEE 569

                   ....*....
gi 1720400152  949 KITRVLELE 957
Cdd:PRK02224   570 AREEVAELN 578
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
725-965 1.67e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 55.50  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  725 LEEHNAAMKDQLKLQEKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSqirQLQHDREEFYNQSQELQTKL----EDCR 800
Cdd:pfam05483  504 LTQEASDMTLELKKHQEDI----INCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLdkseENAR 576
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  801 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFL-------NRQLLVLG-EVNELYLEqLQSkhpdTTKE 872
Cdd:pfam05483  577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaeNKQLNAYEiKVNKLELE-LAS----AKQK 651
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  873 VEMMKTAYRKELEKNR---SHLLQQNQRLDASQRRVLELESLLAKK-DHLLLEQKKYLEDVKSQ-------ASGQLLAAE 941
Cdd:pfam05483  652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHKIAEMVALMEKHKHQydkiieeRDSELGLYK 731
                          250       260
                   ....*....|....*....|....
gi 1720400152  942 SRYEAQRKITRVLELEILDLYGRL 965
Cdd:pfam05483  732 NKEQEQSSAKAALEIELSNIKAEL 755
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
748-967 1.74e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.77  E-value: 1.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  748 VSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQV 827
Cdd:COG4942     13 LAAAAQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  828 SQKLSNSE-SVQQQMEFLNRQLLVL---GEVNELYLEQLQSKHPDTTKEVEMMK--TAYRKE----LEKNRSHLLQQNQR 897
Cdd:COG4942     89 EKEIAELRaELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREqaeeLRADLAELAALRAE 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  898 LDASQRrvlELESLLAKkdhlLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 967
Cdd:COG4942    169 LEAERA---ELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
735-983 1.93e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  735 QLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmvtqlhsqIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKAN 814
Cdd:COG1196    219 KEELKELEAELLLLKLRELEAELEELEAE-----------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  815 NKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQ 894
Cdd:COG1196    288 AEE---YELLAELARLEQDIARLEERRRELEERLEELEEELAE-LEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  895 NQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLRKL 974
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                   ....*....
gi 1720400152  975 EEDRAEAAE 983
Cdd:COG1196    444 LEEAAEEEA 452
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
740-949 2.58e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.45  E-value: 2.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  740 EKDIQMWKVSLQKEQARYSQLQEQRDTM---VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNK 816
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  817 VCHTELLLSQVSQkLSNSESVQqqmEFLNRQllvlgevneLYLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQ 896
Cdd:COG3883     95 LYRSGGSVSYLDV-LLGSESFS---DFLDRL---------SALSKIADADADLLEELK----ADKAELEAKKAELEAKLA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720400152  897 RLDASQRrvlELESLLAKKDHLLLEQKKYLEDVKSQASgQLLAAESRYEAQRK 949
Cdd:COG3883    158 ELEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEA-AAEAQLAELEAELA 206
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
711-968 2.69e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.14  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  711 RNRRLLRKVIRAAALEEHNAAMkdqLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLH---SQIRQLQHDREEFYN 787
Cdd:COG4372      4 LGEKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEqleEELEQARSELEQLEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  788 QSQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLsnsESVQQQMEFLNRQllvlgevnelyLEQLQSKHP 867
Cdd:COG4372     81 ELEELNEQLQAAQAELAQAQEELESLQEE-------AEELQEEL---EELQKERQDLEQQ-----------RKQLEAQIA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  868 DTTKEVEmMKTAYRKELEKNRSHLLQQNQRLDASQRRvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQ 947
Cdd:COG4372    140 ELQSEIA-EREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
                          250       260
                   ....*....|....*....|.
gi 1720400152  948 RKITRVLELEILDLYGRLEKD 968
Cdd:COG4372    218 EELLEAKDSLEAKLGLALSAL 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
681-900 2.75e-07

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: 55.06  E-value: 2.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  681 SDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIRAAALEEHNAAMKDQLKLQEK---DIQMWKVSLQKEQAR 756
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEA 888
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  757 YSQLQEQRDTMVTQlhsqIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVEL----KKANNKVCHT-ELLLSQVSQKL 831
Cdd:TIGR02168  889 LALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTlEEAEALENKIE 964
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720400152  832 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKhpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDA 900
Cdd:TIGR02168  965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEEL-----KERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
738-967 4.81e-07

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: 54.29  E-value: 4.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  738 LQEKDIQMWKVSLQKEQA-RYSQLQEQRDTM--------VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRV 808
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAeRYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  809 ELKKANNKVCHTELLLSQVSQKLSNSES----VQQQMEFLNRQLLVLgevnELYLEQLQSKHPDTTKEVEMMKTAYrKEL 884
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQqkqiLRERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKL-EEL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  885 EKNrshLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ---ASGQLLAAESRYEA-QRKITRVLElEILD 960
Cdd:TIGR02168  350 KEE---LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERlEDRRERLQQ-EIEE 425

                   ....*..
gi 1720400152  961 LYGRLEK 967
Cdd:TIGR02168  426 LLKKLEE 432
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
721-972 7.60e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 7.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  721 RAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE---EFYNQSQELQTKLE 797
Cdd:PRK02224   476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAE 554
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  798 DCRNMIAELRVELKKANNKV--CHTELL--------LSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHp 867
Cdd:PRK02224   555 EKREAAAEAEEEAEEAREEVaeLNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR- 633
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  868 DTTKEVEmmktayrKELEKNRSHLLQQN-QRLDASQRRVLE-LESLLAKKDHLL---------LEQKKYLEDVKSQASGQ 936
Cdd:PRK02224   634 ERKRELE-------AEFDEARIEEAREDkERAEEYLEQVEEkLDELREERDDLQaeigaveneLEELEELRERREALENR 706
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1720400152  937 LLAAESRYEaqrkitRVLELEilDLYGRLEKDGRLR 972
Cdd:PRK02224   707 VEALEALYD------EAEELE--SMYGDLRAELRQR 734
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
676-967 1.52e-06

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: 52.76  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  676 GGS--PPSDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKdQLKLQEKDIQMwkvsLQKE 753
Cdd:TIGR02169  657 GGSraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIEQ----LEQE 731
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  754 QARYSQLQEQrdtmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL-----LLSQVS 828
Cdd:TIGR02169  732 EEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeiqaELSKLE 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  829 QKLSNSESVQQQME-FLNRQLLVLG----EVNEL--YLEQLQSKHPDTTKEVEMMKTAYRK-------------ELEKNR 888
Cdd:TIGR02169  805 EEVSRIEARLREIEqKLNRLTLEKEylekEIQELqeQRIDLKEQIKSIEKEIENLNGKKEEleeeleeleaalrDLESRL 884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  889 SHLLQQNQRLDAS----QRRVLELESLLAKKDHLLLEQKKYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEILDLY 962
Cdd:TIGR02169  885 GDLKKERDELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVE 964

                   ....*
gi 1720400152  963 GRLEK 967
Cdd:TIGR02169  965 EEIRA 969
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
704-958 1.62e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 52.66  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  704 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQeqrdtmvtqlhsQIRQLQHDRE 783
Cdd:TIGR00618  189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT------------QKREAQEEQL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  784 EFYNQSQELQTKLEDCRNMIAELRvELKKANNKVCHTELL------LSQVSQKLSNS-----------ESVQQQMEFLNR 846
Cdd:TIGR00618  257 KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPLaahikaVTQIEQQAQRIhtelqskmrsrAKLLMKRAAHVK 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  847 QLLVLGEVNELyLEQLQSKHPDTTKEVEmMKTAYRKELEKN---RSHLLQQNQRLDASQRRvleLESLLAKKDHLLLEQK 923
Cdd:TIGR00618  336 QQSSIEEQRRL-LQTLHSQEIHIRDAHE-VATSIREISCQQhtlTQHIHTLQQQKTTLTQK---LQSLCKELDILQREQA 410
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1720400152  924 KYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEI 958
Cdd:TIGR00618  411 TIDTRTSAFRDlqGQLAHAKKQQELQQRYAELCAAAI 447
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
715-955 2.71e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 51.65  E-value: 2.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  715 LLRKVIRAAALEEH-NAAMKDQLKL-QEKDIQMWKvsLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQ---- 788
Cdd:pfam05483  305 LQRSMSTQKALEEDlQIATKTICQLtEEKEAQMEE--LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkii 382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  789 SQELQTK---LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQklsnSESVQQQMEFLNRQLLVLGEVNELYLEQLQSK 865
Cdd:pfam05483  383 TMELQKKsseLEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ----FEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  866 HPDTT-------KEVEMMKTayrkELEKNRshlLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDV---KSQASG 935
Cdd:pfam05483  459 LTAIKtseehylKEVEDLKT----ELEKEK---LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEER 531
                          250       260
                   ....*....|....*....|
gi 1720400152  936 QLLAAESRYEAQRKITRVLE 955
Cdd:pfam05483  532 MLKQIENLEEKEMNLRDELE 551
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
712-863 3.86e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 3.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  712 NRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYSQLQEQRDTMVTQL---HSQIRQLQHDREEFY 786
Cdd:COG3206    225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720400152  787 NQ-SQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 863
Cdd:COG3206    305 AQlQQEAQRILASLEAELEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
701-968 4.96e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 4.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  701 ERFKRQQHALRNRrLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQ 777
Cdd:COG4372     41 DKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEE 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  778 LQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSN------SESVQQQMEFLNRQLLVL 851
Cdd:COG4372    120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeaEQALDELLKEANRNAEKE 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  852 GEVNELYLEQLQSKHPdTTKEVEMMKTAYRKELEKNRSHLLQQNQRL-DASQRRVLELESLLAKKDHLLLEQKKYLEDVK 930
Cdd:COG4372    200 EELAEAEKLIESLPRE-LAEELLEAKDSLEAKLGLALSALLDALELEeDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1720400152  931 SQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKD 968
Cdd:COG4372    279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
712-958 5.06e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.92  E-value: 5.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  712 NRRLLR-KV--IRAAALEEHNAaMKDQLKLQEKDI-QMWKV----SLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE 783
Cdd:pfam13868   12 NSKLLAaKCnkERDAQIAEKKR-IKAEEKEEERRLdEMMEEererALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  784 EFYNQS-QELQTKLEDCRNMIAE-LRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLvlgevneLYLEQ 861
Cdd:pfam13868   91 EEYEEKlQEREQMDEIVERIQEEdQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-------EYLKE 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  862 LQSKhpDTTKEVEMMKTAYRKELEKNRshLLQQNQRLDASQRrvlELESLLAKkdhLLLEQ------KKYLEDVKSQASG 935
Cdd:pfam13868  164 KAER--EEEREAEREEIEEEKEREIAR--LRAQQEKAQDEKA---ERDELRAK---LYQEEqerkerQKEREEAEKKARQ 233
                          250       260
                   ....*....|....*....|...
gi 1720400152  936 QLLAAESRYEAQRKITRVLELEI 958
Cdd:pfam13868  234 RQELQQAREEQIELKERRLAEEA 256
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
744-959 6.76e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 6.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  744 QMWKVSLQKEQARYSQLQEQRDTM-VTQLHSQIRQLQHDREEfYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL 822
Cdd:COG4717     45 AMLLERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  823 LLSQVSQklsnsesvQQQMEFLNRQLLVLGEVnelyLEQLQSKHpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQ 902
Cdd:COG4717    124 LLQLLPL--------YQELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLAT 190
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720400152  903 RRVL-----ELESLLAKKDHLLLEQKKyLEDVKSQASGQLLAAESRYEAQRKITRVLELEIL 959
Cdd:COG4717    191 EEELqdlaeELEELQQRLAELEEELEE-AQEELEELEEELEQLENELEAAALEERLKEARLL 251
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
768-967 1.06e-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: 50.06  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  768 VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCR-------NMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQ 840
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  841 MEFLNRQL------LVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRV--------- 905
Cdd:TIGR02168  763 IEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaterrled 842
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720400152  906 ---------LELESLLAKKDHL------LLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 967
Cdd:TIGR02168  843 leeqieelsEDIESLAAEIEELeelieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
682-961 1.20e-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: 49.67  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  682 DELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDiqmwkvsLQKEQArysQLQ 761
Cdd:TIGR02168  719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-------AEAEIE---ELE 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  762 EQRDTMVTQLHSQIRQLQHDREEFYNQS---QELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQ 838
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI---EELE 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  839 QQMEFLNRQL---LVLGEVNELYLEQLQSKHPDTTKEVEMM---KTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLL 912
Cdd:TIGR02168  866 ELIEELESELealLNERASLEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720400152  913 AKKDHLLLE--QKKYLEDVKSQAsgqllaaesryEAQRKITRvLELEILDL 961
Cdd:TIGR02168  946 SEEYSLTLEeaEALENKIEDDEE-----------EARRRLKR-LENKIKEL 984
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
726-930 1.92e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  726 EEHNAAMKDQLKLQEKDIQMWKvsLQKEQARYSQLQ------EQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDC 799
Cdd:TIGR00618  660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  800 RNMIAELRVELKK-ANNKVCHTELLLSQVS-------QKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTK 871
Cdd:TIGR00618  738 EDALNQSLKELMHqARTVLKARTEAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720400152  872 EVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVK 930
Cdd:TIGR00618  818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
714-973 2.20e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  714 RLLRKVIRaaaLEEHNAAMKDQLKLQeKDIQMWKVSLQKEQARYSQLQEQRDTM----------VTQLHSQIRQLqhdRE 783
Cdd:PRK03918   149 KVVRQILG---LDDYENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPEL---RE 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  784 EFYNQSQELQtKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELY--LEQ 861
Cdd:PRK03918   222 ELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYikLSE 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  862 LQSKHPDTTKEVEMMKTAYR---KELEKNRSHLLQQNQRLDASQRRVLELESLLA--KKDHLLLEQ----KKYLEDVKSQ 932
Cdd:PRK03918   301 FYEEYLDELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEakakKEELERLKKR 380
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1720400152  933 ASGQLLA-AESRYEAQRKITRVLELEILDLYGRLekdGRLRK 973
Cdd:PRK03918   381 LTGLTPEkLEKELEELEKAKEEIEEEISKITARI---GELKK 419
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
677-892 4.16e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  677 GSPPSDELRTLRDQL----LLLHNQLLYERFKRQQHALRNRRllrkviraAALEEHNAAMKDQLKLQEKDIQMWKVSLQK 752
Cdd:COG4717     63 GRKPELNLKELKELEeelkEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQEL 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  753 EQARySQLQEqrdtmvtqLHSQIRQLQHDREEFynqsQELQTKLEDCRNMIAELRVELKKANNKVchTELLLSQVSQKLS 832
Cdd:COG4717    135 EALE-AELAE--------LPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAE 199
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  833 NSESVQQQMEFLNRQLlvlgEVNELYLEQLQSKHPDTtkEVEMMKTAYRKELEKNRSHLL 892
Cdd:COG4717    200 ELEELQQRLAELEEEL----EEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLL 253
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
735-972 4.57e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.79  E-value: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  735 QLKLQEKDIQMWKVSLQKE-QARYSQLQEQRDTMVTQlHSQIRQLQHDREEFynqSQELQTKLEDCRNMIAElrvelkka 813
Cdd:pfam05483   82 KLYKEAEKIKKWKVSIEAElKQKENKLQENRKIIEAQ-RKAIQELQFENEKV---SLKLEEEIQENKDLIKE-------- 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  814 NNKVCHTELLLSQVSQKlsnSESVQQQMEFlNRQllvlgEVNELYLeqlqskhpDTTKEVEMMKTAYrKELEknrshLLQ 893
Cdd:pfam05483  150 NNATRHLCNLLKETCAR---SAEKTKKYEY-ERE-----ETRQVYM--------DLNNNIEKMILAF-EELR-----VQA 206
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720400152  894 QNQRLDASqrrvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLElEILDLYGRLEKDGRLR 972
Cdd:pfam05483  207 ENARLEMH----FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE-ESRDKANQLEEKTKLQ 280
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
701-955 5.20e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 5.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  701 ERFKRQQHALRNR-RLLRKVIRAAALEEHNAAMK----------DQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVT 769
Cdd:COG4717    105 EELEAELEELREElEKLEKLLQLLPLYQELEALEaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLE 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  770 QL----HSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL----------------LLSQVSQ 829
Cdd:COG4717    185 QLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeerlkearlllliaaaLLALLGL 264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  830 KLSNSESVQQQMEFLnrqLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEK----------------NRSHLLQ 893
Cdd:COG4717    265 GGSLLSLILTIAGVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeeleellaalglppdlSPEELLE 341
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720400152  894 QNQRLDASQRRVLELESLL--AKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLE 955
Cdd:COG4717    342 LLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE 405
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
700-953 1.47e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  700 YERF-KRQQHALRNRRLL-----RKViraAALEEhnaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDT------- 766
Cdd:COG4913    587 GTRHeKDDRRRIRSRYVLgfdnrAKL---AALEA-------ELAELEEELAEAEERLEALEAELDALQERREAlqrlaey 656
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  767 -----MVTQLHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQ 838
Cdd:COG4913    657 swdeiDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  839 QQMEFLNRQLLVLgEVNELYLEQLQSKHPDTtkevemMKTAYRKELEKNRSHLLQQNQRL------------------DA 900
Cdd:COG4913    737 EAAEDLARLELRA-LLEERFAAALGDAVERE------LRENLEERIDALRARLNRAEEELeramrafnrewpaetadlDA 809
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  901 SQRRVLELESLLAK-KDHLLLEQKKYLEDVKSQASGQLLA------AESRYEAQRKITRV 953
Cdd:COG4913    810 DLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVAdllsklRRAIREIKERIDPL 869
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
710-958 2.69e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  710 LRNRRLLRKVIRAAALEEHN-----------AAMKDQLKLQ-EKDIQMWKVS--------------------------LQ 751
Cdd:COG3206     90 LKSRPVLERVVDKLNLDEDPlgeeasreaaiERLRKNLTVEpVKGSNVIEISytspdpelaaavanalaeayleqnleLR 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  752 KEQARYSQ--LQEQRDtmvtQLHSQIRQLQHDREEF---------YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHT 820
Cdd:COG3206    170 REEARKALefLEEQLP----ELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  821 ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDttkevemMKTAyRKELEKNRSHLLQQNQRLDA 900
Cdd:COG3206    246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL-SARYTPNHPD-------VIAL-RAQIAALRAQLQQEAQRILA 316
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720400152  901 SQRRvlELESLLAKKDHLLLEQKKYLEDVKS--QASGQLLAAESRYEAQRKI-----TRVLELEI 958
Cdd:COG3206    317 SLEA--ELEALQAREASLQAQLAQLEARLAElpELEAELRRLEREVEVARELyesllQRLEEARL 379
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
722-817 2.99e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 2.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152   722 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSqlQEQRDTMVTQLHSQIRQLQHDREEFynqSQELQTKLedcRN 801
Cdd:smart00935   20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
                            90
                    ....*....|....*.
gi 1720400152   802 MIAELRVELKKANNKV 817
Cdd:smart00935   92 ELQKILDKINKAIKEV 107
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
723-864 5.71e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 41.09  E-value: 5.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  723 AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVtQLHSQ-IRQLQHDREEFynqsQELQTKledcrn 801
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYEREL-VLHAEdIKALQALREEL----NELKAE------ 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720400152  802 mIAELRVELKKANnkvchTELLLSQVS---QKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQS 864
Cdd:pfam07926   73 -IAELKAEAESAK-----AELEESEESweeQK----KELEKELSELEKRIEDLNEQNKLLHDQLES 128
PRK11637 PRK11637
AmiB activator; Provisional
730-921 6.14e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 43.53  E-value: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  730 AAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQhdreefynQSQELQTKLedcrnmiaeLRVE 809
Cdd:PRK11637    71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLE--------QQQAAQERL---------LAAQ 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  810 LKKANNKVCHT--ELLLS-QVSQKlsnSESVQQQMEFLNrqllvlgEVNELYLEQLQSkhpdTTKEVemmkTAYRKELEK 886
Cdd:PRK11637   130 LDAAFRQGEHTglQLILSgEESQR---GERILAYFGYLN-------QARQETIAELKQ----TREEL----AAQKAELEE 191
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1720400152  887 NRSH---LL----QQNQRLD----ASQRRVLELESLLAKKDHLLLE 921
Cdd:PRK11637   192 KQSQqktLLyeqqAQQQKLEqarnERKKTLTGLESSLQKDQQQLSE 237
Filament pfam00038
Intermediate filament protein;
724-949 6.22e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 6.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  724 ALEEHNAAMKDQLK-LQEKdiQMWKVSlQKEQARYSQLQEQRDTMVT------QLHSQIRQLQHDREEFYNQSQELQTKL 796
Cdd:pfam00038   22 FLEQQNKLLETKISeLRQK--KGAEPS-RLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAEDFRQKYEDELNLR 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  797 EDCRNMIAELRVELKKAN-NKVchtELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEM 875
Cdd:pfam00038   99 TSAENDLVGLRKDLDEATlARV---DL---------------EAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  876 --------------MKTAYRKELEKNRSHL----------LQQ-----NQRLDASQRRVLEL----ESLLAKKDHlLLEQ 922
Cdd:pfam00038  161 daarkldltsalaeIRAQYEEIAAKNREEAeewyqskleeLQQaaarnGDALRSAKEEITELrrtiQSLEIELQS-LKKQ 239
                          250       260
                   ....*....|....*....|....*..
gi 1720400152  923 KKYLEDvksqasgQLLAAESRYEAQRK 949
Cdd:pfam00038  240 KASLER-------QLAETEERYELQLA 259
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
701-909 6.29e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 6.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  701 ERFKRQQHALRNRRLLRkviRAAALEEHNAAMKDQLKLQEKDIQMWKvslqkEQARYSQLQEQRDTMVTQ---LHSQIRQ 777
Cdd:COG3206    159 EAYLEQNLELRREEARK---ALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQlseLESQLAE 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  778 LQHDREEFYNQSQELQTKLEDCRNMIAELR--VELKKANNKVCHTELLLSQVSQKLS-NSESVQQqmefLNRQLlvlGEV 854
Cdd:COG3206    231 ARAELAEAEARLAALRAQLGSGPDALPELLqsPVIQQLRAQLAELEAELAELSARYTpNHPDVIA----LRAQI---AAL 303
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720400152  855 NELYLEQLQSKHPDTTKEVEMMKtAYRKELEKNRSHLLQQNQRLDASQRRVLELE 909
Cdd:COG3206    304 RAQLQQEAQRILASLEAELEALQ-AREASLQAQLAQLEARLAELPELEAELRRLE 357
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
753-931 6.73e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.52  E-value: 6.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  753 EQARYSQLQEQR---------------DTMVTQLHS-----QIRQLQHD-------REEFYNQSQ-ELQTKLEDCRNMIA 804
Cdd:pfam05622  242 EELRCAQLQQAElsqadallspssdpgDNLAAEIMPaeireKLIRLQHEnkmlrlgQEGSYRERLtELQQLLEDANRRKN 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  805 ELRVELKKANNKVchTELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNE--LYLEQLQSKHPDTTKEVEmmktayrK 882
Cdd:pfam05622  322 ELETQNRLANQRI--LEL---------------QQQVEELQKALQEQGSKAEdsSLLKQKLEEHLEKLHEAQ-------S 377
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720400152  883 ELEKNRSHLLQQNQRLDAS-QRRVLELESLLAKKDH--LLLEQ--KKYLEDVKS 931
Cdd:pfam05622  378 ELQKKKEQIEELEPKQDSNlAQKIDELQEALRKKDEdmKAMEEryKKYVEKAKS 431
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
702-950 1.01e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  702 RFKRQQHALRNRRLLRKVIRAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQ---EQRDtmvtqlhsqiRQL 778
Cdd:pfam17380  384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  779 QHDREEfynqSQELQTKLEDCRNMIAELRvelkkannkvchtelllsQVSQKLSNSESVQQQMEFLNRQLLvlgevnELY 858
Cdd:pfam17380  449 ERVRLE----EQERQQQVERLRQQEEERK------------------RKKLELEKEKRDRKRAEEQRRKIL------EKE 500
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  859 LEQLQSKHPDTTKEVEMMKtayrKELEKNRSHLLQQNQRLDASQRRVLELEsllakkdhllLEQKKYLEDVKSQAS---G 935
Cdd:pfam17380  501 LEERKQAMIEEERKRKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKATeerS 566
                          250
                   ....*....|....*
gi 1720400152  936 QLLAAESRYEAQRKI 950
Cdd:pfam17380  567 RLEAMEREREMMRQI 581
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
706-811 1.03e-03

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: 41.82  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  706 QQHALRNRRLLRKViraAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYSQLQEQRDTMvtQLHSQ-----IRQLQH 780
Cdd:pfam13851   50 SEIQQENKRLTEPL---QKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1720400152  781 DREEFYNQS----QELQTKLEdCRNMIAELRVELK 811
Cdd:pfam13851  121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
759-928 1.31e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 41.29  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  759 QLQEQRDTMVTQLHSQIRQLQHDREE----FYNQSQELQTKLEDCRNMIAELRVELK--------KANNKVCHTELLLSQ 826
Cdd:pfam14988   15 EKQKKIEKLWNQYVQECEEIERRRQElasrYTQQTAELQTQLLQKEKEQASLKKELQalrpfaklKESQEREIQDLEEEK 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  827 VSQKLSNSESVQQ-QMEFLNRQLLVLGEVNELYLEQL-QSKHPDTTKEVEMMKTAYRK--------------ELEKNRSH 890
Cdd:pfam14988   95 EKVRAETAEKDREaHLQFLKEKALLEKQLQELRILELgERATRELKRKAQALKLAAKQalsefcrsikrenrQLQKELLQ 174
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1720400152  891 LLQQNQRLDASQRRvleleslLAKKDHLLLEQKKYLED 928
Cdd:pfam14988  175 LIQETQALEAIKSK-------LENRKQRLKEEQWYLEA 205
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
701-960 1.42e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 42.87  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  701 ERFKRQQHALRNRRLLRKVIRA---------AALEEHNAAMKDQLKL-----------------QEKDIQMWkvslQKEQ 754
Cdd:PRK10246   606 EEHERQLRLLSQRHELQGQIAAhnqqiiqyqQQIEQRQQQLLTALAGyaltlpqedeeaswlatRQQEAQSW----QQRQ 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  755 ARYSQLQEQ-------------RDTMVTQ------------------LHSQIRQLQHDREEFYNQSQELQTKLE------ 797
Cdd:PRK10246   682 NELTALQNRiqqltplletlpqSDDLPHSeetvaldnwrqvheqclsLHSQLQTLQQQDVLEAQRLQKAQAQFDtalqas 761
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  798 ---DCRNMIAEL-------RVELKKAN--NKVCHTELLLSQVSQKLSnsESVQQQMEFLNRQLLVlgEVNELYLEQL-QS 864
Cdd:PRK10246   762 vfdDQQAFLAALldeetltQLEQLKQNleNQRQQAQTLVTQTAQALA--QHQQHRPDGLDLTVTV--EQIQQELAQLaQQ 837
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  865 KHPDTTKEVEMmktayRKEL---EKNRSHLLQQNQRLDASQRRVLE---LESLLAKK--DHLL-LEQKKYLEDVKSQASG 935
Cdd:PRK10246   838 LRENTTRQGEI-----RQQLkqdADNRQQQQALMQQIAQATQQVEDwgyLNSLIGSKegDKFRkFAQGLTLDNLVWLANQ 912
                          330       340
                   ....*....|....*....|....*
gi 1720400152  936 QLLAAESRYEAQRKITRVLELEILD 960
Cdd:PRK10246   913 QLTRLHGRYLLQRKASEALELEVVD 937
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
705-961 1.64e-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: 42.74  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  705 RQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLqhdree 784
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI------ 784
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  785 fynqsQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLLVLGEV---NEL 857
Cdd:TIGR02168  785 -----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaATERRLEDLEEQIEELSEDiesLAA 859
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  858 YLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVksqasgQL 937
Cdd:TIGR02168  860 EIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------EL 929
                          250       260
                   ....*....|....*....|....
gi 1720400152  938 LAAESRYEAQRKITRVLELEILDL 961
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLSEEYSLTL 953
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
704-946 1.68e-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: 42.50  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  704 KRQQHALRnRRLLRKVIRAAALEEH-----NAAMKDQLKLQEKDIQMWK----VSLQKEQARYSQLQEQRDTMVTQLHSQ 774
Cdd:pfam10174  481 KEKVSALQ-PELTEKESSLIDLKEHasslaSSGLKKDSKLKSLEIAVEQkkeeCSKLENQLKKAHNAEEAVRTNPEINDR 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  775 IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTE-LLLSQV---SQKLSNSESVQQQMEFLNRQLLV 850
Cdd:pfam10174  560 IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELEsLTLRQMkeqNKKVANIKHGQQEMKKKGAQLLE 639
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  851 LGEVNElylEQLQSKHPDTTKEvEMMKtayrkELEKNRSHLLQQNQRLDASQRRVLELESLLAKkdhLLLEQKKYLEDV- 929
Cdd:pfam10174  640 EARRRE---DNLADNSQQLQLE-ELMG-----ALEKTRQELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIl 707
                          250
                   ....*....|....*....
gi 1720400152  930 --KSQAsgqLLAAESRYEA 946
Cdd:pfam10174  708 emKQEA---LLAAISEKDA 723
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
832-943 1.94e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 39.97  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  832 SNSESVQQQMEFLNRQLLVLGEVNE-LYLEQLQSKhpdttKEVEMMK------TAYRKELEKNRSHLLQQ----NQRLDA 900
Cdd:pfam10473   17 RKADSLKDKVENLERELEMSEENQElAILEAENSK-----AEVETLKaeieemAQNLRDLELDLVTLRSEkenlTKELQK 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720400152  901 SQRRVLELESLLAKKDHLL--LEQKKYLEDVKSQASGQLLAAESR 943
Cdd:pfam10473   92 KQERVSELESLNSSLENLLeeKEQEKVQMKEESKTAVEMLQTQLK 136
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
711-921 2.66e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.13  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  711 RNRRLLRKVIRAAALEEHNA-AMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtQLHSQIRQLQHDREefyNQS 789
Cdd:pfam12128  330 QHGAFLDADIETAAADQEQLpSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---QNNRDIAGIKDKLA---KIR 403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  790 QELQTKLEDCRNMI----AELRVELKKANNKVCHTELLLS--------QVSQKLSNSESVQQQmeflnrqllvlgEVNEL 857
Cdd:pfam12128  404 EARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYRLKsrlgelklRLNQATATPELLLQL------------ENFDE 471
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720400152  858 YLEQLQSKHPDTTKEVEMMK---TAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 921
Cdd:pfam12128  472 RIERAREEQEAANAEVERLQselRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH 538
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
704-972 2.84e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  704 KRQQHALRNRRLLRKVIRAAaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRdtmvtqlHSQIRQLQHDRE 783
Cdd:pfam13868   62 EKEEERKEERKRYRQELEEQ-IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK-------LEKQRQLREEID 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  784 EFYNQSQEL------QTKLEDCRNM------------IAELRVELKKANnkvchtELLLSQVSQKLSNSESVQQQMEFLn 845
Cdd:pfam13868  134 EFNEEQAEWkelekeEEREEDERILeylkekaereeeREAEREEIEEEK------EREIARLRAQQEKAQDEKAERDEL- 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  846 RQLLVLGEVN----ELYLEQLQSKHpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDhLLLE 921
Cdd:pfam13868  207 RAKLYQEEQErkerQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE-QEEA 281
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720400152  922 QKKYLEDVKSQASGQLLAAESryEAQRKITRVLELEILDLYGRLEKDGRLR 972
Cdd:pfam13868  282 EKRRMKRLEHRRELEKQIEER--EEQRAAEREEELEEGERLREEEAERRER 330
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
722-973 3.30e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  722 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQArysQLQEQRDTMvtqlhSQIRQ-LQHDREEFYNQSQELQTKLEDCR 800
Cdd:pfam01576  355 TQALEELTEQL-EQAKRNKANLEKAKQALESENA---ELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESE 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  801 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSesvQQQMEFLNRQllvLGEVNELYLEQLQSKHPDTTKevemmktay 880
Cdd:pfam01576  426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQ---LQDTQELLQEETRQKLNLSTR--------- 490
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  881 RKELEKNRSHLLQQNQRLDASQRRV-LELESLLAKkdhlLLEQKKYLEDVksqaSGQLLAAEsryEAQRKITRVLELEIL 959
Cdd:pfam01576  491 LRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQ----LSDMKKKLEED----AGTLEALE---EGKKRLQRELEALTQ 559
                          250       260
                   ....*....|....*....|.
gi 1720400152  960 DL------YGRLEK-DGRLRK 973
Cdd:pfam01576  560 QLeekaaaYDKLEKtKNRLQQ 580
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
701-915 3.36e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  701 ERFKRQQHALRNRRLLRKVIRA--AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 778
Cdd:COG4942     34 QEIAELEKELAALKKEEKALLKqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  779 Q--------------HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchTELLLSQVSQKLSNSESVQQQMEFl 844
Cdd:COG4942    114 YrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAA- 189
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720400152  845 nrqllvlgevnelyLEQLQSKHPDTTKEVEMMKTAYRKELEKnrshLLQQNQRLDASQRRVLELESLLAKK 915
Cdd:COG4942    190 --------------LEALKAERQKLLARLEKELAELAAELAE----LQQEAEELEALIARLEAEAAAAAER 242
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
787-968 3.39e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  787 NQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 862
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  863 QSKHPDTTKEV-EMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLElesllakkDHLLLEQKKYLEDVKSQASgQLLAAE 941
Cdd:COG4942     96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLA-ELAALR 166
                          170       180
                   ....*....|....*....|....*..
gi 1720400152  942 SRYEAQRKITRVLELEILDLYGRLEKD 968
Cdd:COG4942    167 AELEAERAELEALLAELEEERAALEAL 193
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
704-921 4.06e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 40.36  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  704 KRQQHALRNRRLlRKVIRAAAleehnaamKDQLKLQEKDIQMWKVSLQKEQARYSQL-QEQRDTMVTQLHSQIRQLQHDR 782
Cdd:pfam12795   31 KIDASKQRAAAY-QKALDDAP--------AELRELRQELAALQAKAEAAPKEILASLsLEELEQRLLQTSAQLQELQNQL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  783 EEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchteLLLSQVSQK-LSNSESVQQQMEflnRQLLVLgEVNELYLEQ 861
Cdd:pfam12795  102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNR-----LNGPAPPGEpLSEAQRWALQAE---LAALKA-QIDMLEQEL 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720400152  862 LQSkhpdttkevEMMKTAYRKELEKNRSHLLQQNQRLDA-----SQRRVLELESLLAKKDHLLLE 921
Cdd:pfam12795  173 LSN---------NNRQDLLKARRDLLTLRIQRLEQQLQAlqellNEKRLQEAEQAVAQTEQLAEE 228
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
721-848 4.22e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  721 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQE-----------QRDTMVTQLHSQ----IRQLQHDREEF 785
Cdd:COG3883     66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADAdadlLEELKADKAEL 145
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720400152  786 YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQQQMEFLNRQL 848
Cdd:COG3883    146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQLAELEAEL 205
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
733-932 4.84e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 4.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  733 KDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVE 809
Cdd:TIGR04523  418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  810 LKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-----------LNRQLLVLGEV--NELYLEQLQSKHpdttKEVEMM 876
Cdd:TIGR04523  498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESekkekeskisdLEDELNKDDFElkKENLEKEIDEKN----KEIEEL 573
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720400152  877 KTAYrKELEKNRShllQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 932
Cdd:TIGR04523  574 KQTQ-KSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
732-957 4.88e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.10  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  732 MKDQLKLQEkdiQMWKVSLQKEQ----ARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNM----I 803
Cdd:COG5185    346 EQGQESLTE---NLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqI 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  804 AELRVELKKANNKVchtelllsQVSQKLSN---SESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEMMKT-- 878
Cdd:COG5185    423 EELQRQIEQATSSN--------EEVSKLLNeliSELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESrv 494
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  879 -AYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELE 957
Cdd:COG5185    495 sTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELT 574
PRK05563 PRK05563
DNA polymerase III subunits gamma and tau; Validated
764-924 5.16e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235505 [Multi-domain]  Cd Length: 559  Bit Score: 41.01  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  764 RDTMVTQLHSQ---IRQLQHDREEFYNQSQELQTK-LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNS----- 834
Cdd:PRK05563   290 RDLLLVKTSPEleiLDESTENDELFKELSEKLDIErLYRMIDILNDAQQQIKWTNQPRIYLEVALVKLCEQAAASpeydt 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  835 --ESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEV------------EMMKTAYRKELEKNRSH---LLQQNQR 897
Cdd:PRK05563   370 elEVLLQRVEQLEQELKQLKAQPVGVAPEQKEKKKEKKKNKkkkykvprgkiyKVLKEATRQDLELLKNVwgeILESLKA 449
                          170       180
                   ....*....|....*....|....*...
gi 1720400152  898 LDASQRRVL-ELESLLAKKDHLLLEQKK 924
Cdd:PRK05563   450 QRKSLRALLvNSEPVAASEDTVVLAFEY 477
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
759-844 6.36e-03

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 39.17  E-value: 6.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  759 QLQEQRdtMVTQ-LHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELK-KANNKVCHTELLLSQVSQKLSn 833
Cdd:cd16855      9 QLEELR--QRTQeTENDLRNLQQKQESFviqYQESQKIQAQLQQLQQQPQNERIELEqQLQQQKEQLEQLLNAKAQELL- 85
                           90
                   ....*....|.
gi 1720400152  834 sesvQQQMEFL 844
Cdd:cd16855     86 ----QLRMELA 92
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
700-817 7.55e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 7.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  700 YERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQ-EKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 778
Cdd:COG4717    343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdEEEL----RAALEQAEEYQELKEELEELEEQLEELLGEL 418
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720400152  779 QH-----DREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKV 817
Cdd:COG4717    419 EEllealDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
717-906 8.74e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 8.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  717 RKVIRAAALEEHNAAMKDQLKLQEKDIqmwkvslqkEQaRYSQLQEQRdTMVTQLHSQIRQLQHDREEFYNQSQELQTKL 796
Cdd:COG3096    498 RELLRRYRSQQALAQRLQQLRAQLAEL---------EQ-RLRQQQNAE-RLLEEFCQRIGQQLDAAEELEELLAELEAQL 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  797 EDCRNMIAE-------LRVELKKANNKVchTEL----------------LLSQVSQKLSNSESVQQQMEFLnrqllvlge 853
Cdd:COG3096    567 EELEEQAAEaveqrseLRQQLEQLRARI--KELaarapawlaaqdalerLREQSGEALADSQEVTAAMQQL--------- 635
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720400152  854 vnelyLEQLqskhpdttkevemmktayrKELEKNRSHLLQQNQRLDASQRRVL 906
Cdd:COG3096    636 -----LERE-------------------REATVERDELAARKQALESQIERLS 664
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
733-932 9.81e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 9.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  733 KDQLKLQEKDIQmwkvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKK 812
Cdd:TIGR04523  116 KEQKNKLEVELN----KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  813 ANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGE-VNELY--LEQLQSKHPDTTKEVEMMK---TAYRKELEK 886
Cdd:TIGR04523  192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQqeINEKTTEISNTQTQLNQLKdeqNKIKKQLSE 271
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1720400152  887 NRSHLLQQNQRLDASQRRVLELESLLAKkdhllLEQKK---YLEDVKSQ 932
Cdd:TIGR04523  272 KQKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKeqdWNKELKSE 315
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
725-932 9.81e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 9.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  725 LEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQEL-----QTKleDC 799
Cdd:TIGR04523  431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneEKK--EL 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  800 RNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYLEQ-----LQSKHP 867
Cdd:TIGR04523  509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQTQkslkkKQEEKQ 588
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720400152  868 DTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 932
Cdd:TIGR04523  589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
702-961 9.92e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.03  E-value: 9.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  702 RFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHD 781
Cdd:TIGR00606  828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  782 REE----------FYNQSQELQTKLEDcRNMIAELRVEL--KKANNKVCHTELL------------------LSQVSQKL 831
Cdd:TIGR00606  908 KEQdspletflekDQQEKEELISSKET-SNKKAQDKVNDikEKVKNIHGYMKDIenkiqdgkddylkqketeLNTVNAQL 986
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400152  832 SNSESVQQQME---FLNRQLLVLGEVNELYL-EQL-QSKHPDTTKEVEMMKTAYRKELEKNR-SHLLQQNQRLDASQRRV 905
Cdd:TIGR00606  987 EECEKHQEKINedmRLMRQDIDTQKIQERWLqDNLtLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLI 1066
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720400152  906 LELESLLAKKDHLLLEQKKYLEdvKSQASGQLLAAESRYEAQRKITRVLELEILDL 961
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFK--KELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
 
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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