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Conserved domains on  [gi|24497607|ref|NP_714940|]
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nuclear pore glycoprotein p62 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nsp1_C pfam05064
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ...
328-429 2.71e-46

Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region of Nsp1 is involved in binding Nup82.


:

Pssm-ID: 461540 [Multi-domain]  Cd Length: 114  Bit Score: 157.47  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   328 MTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLL 407
Cdd:pfam05064  13 LKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLDYVESQQDELESLL 92
                          90       100
                  ....*....|....*....|..
gi 24497607   408 SPLEELVKEQSGTIYLQHADEE 429
Cdd:pfam05064  93 DNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 super family cl37900
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
1-255 4.68e-09

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


The actual alignment was detected with superfamily member pfam15967:

Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 58.91  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607     1 MSGFNFGGTGAPT----GGFTFGTAKTAtttpatgfsfSTSGTGGFNFGAPFQPATSTPSTGLFSLATQTPATQttgftf 76
Cdd:pfam15967   1 MSGFSFGGGPGSTatagGGFSFGAAAAS----------NPGSTGGFSFGTLGAAPAATATTTTATLGLGGGLFG------ 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    77 gtatlASGGTGFSLGigasklnlsNTAATPAMANPSGFGLGSSNLTNAisstvtssqgtAPTGFVFGPSTtsvaPATTSG 156
Cdd:pfam15967  65 -----QKPATGFTFG---------TPASSTAATGPTGLTLGTPAATTA-----------ASTGFSLGFNK----PAASAT 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   157 GFSFTGGSTAqPSGFNIGSAGNSAQPTAPATlPFTPATPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTSSATTG 236
Cdd:pfam15967 116 PFSLPASSTS-GGGLSLGSVLTSTAAQQGAT-GFTLNLGGTPATTTAVSTGLSLGSTLTSLGGSLFQNTNSTGLGQTTLG 193
                         250
                  ....*....|....*....
gi 24497607   237 LSLCTPVTTAGAPTAGTQG 255
Cdd:pfam15967 194 LTLLATSTAPVSAPAASEG 212
RecN super family cl33912
DNA repair ATPase RecN [Replication, recombination and repair];
374-515 2.36e-04

DNA repair ATPase RecN [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0497:

Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 374 SLHREVEKVKLDQKRLDQELDFILSQQKELEDL-LSP--LEELVKEQSgtiYLQHADEEREKTYKLAE-------NIDAQ 443
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAaLQPgeEEELEEERR---RLSNAEKLREALQEALEalsggegGALDL 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 444 LKRMAQDLKDIIEHLNTSGAPADT----SDPLQQICKILNAHMDS-------LQWIDQ-NSAL--LQRK----VEEVTKV 505
Cdd:COG0497 246 LGQALRALERLAEYDPSLAELAERlesaLIELEEAASELRRYLDSlefdperLEEVEErLALLrrLARKygvtVEELLAY 325
                       170
                ....*....|
gi 24497607 506 CEGRRKEQER 515
Cdd:COG0497 326 AEELRAELAE 335
 
Name Accession Description Interval E-value
Nsp1_C pfam05064
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ...
328-429 2.71e-46

Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region of Nsp1 is involved in binding Nup82.


Pssm-ID: 461540 [Multi-domain]  Cd Length: 114  Bit Score: 157.47  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   328 MTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLL 407
Cdd:pfam05064  13 LKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLDYVESQQDELESLL 92
                          90       100
                  ....*....|....*....|..
gi 24497607   408 SPLEELVKEQSGTIYLQHADEE 429
Cdd:pfam05064  93 DNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
1-255 4.68e-09

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 58.91  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607     1 MSGFNFGGTGAPT----GGFTFGTAKTAtttpatgfsfSTSGTGGFNFGAPFQPATSTPSTGLFSLATQTPATQttgftf 76
Cdd:pfam15967   1 MSGFSFGGGPGSTatagGGFSFGAAAAS----------NPGSTGGFSFGTLGAAPAATATTTTATLGLGGGLFG------ 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    77 gtatlASGGTGFSLGigasklnlsNTAATPAMANPSGFGLGSSNLTNAisstvtssqgtAPTGFVFGPSTtsvaPATTSG 156
Cdd:pfam15967  65 -----QKPATGFTFG---------TPASSTAATGPTGLTLGTPAATTA-----------ASTGFSLGFNK----PAASAT 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   157 GFSFTGGSTAqPSGFNIGSAGNSAQPTAPATlPFTPATPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTSSATTG 236
Cdd:pfam15967 116 PFSLPASSTS-GGGLSLGSVLTSTAAQQGAT-GFTLNLGGTPATTTAVSTGLSLGSTLTSLGGSLFQNTNSTGLGQTTLG 193
                         250
                  ....*....|....*....
gi 24497607   237 LSLCTPVTTAGAPTAGTQG 255
Cdd:pfam15967 194 LTLLATSTAPVSAPAASEG 212
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
49-249 3.21e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 49.75  E-value: 3.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  49 QPATSTPSTGLFSLATQTPATQTTGFTFGTATLASGGTGFSLGIGASKLNLSNTAATPAMANPSGFGLGSSNLTNAISST 128
Cdd:COG3469  12 AGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 129 V------TSSQGTAPTGFVFGPSTTSVAPATTSGGFSFTGGSTAQPSGFNIGSAGNSAQPTAPATLPFTPATPAATTAGA 202
Cdd:COG3469  92 TsatlvaTSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTT 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24497607 203 TQPAAPTPTATITSTGPSLFASIATAPTSSATTglslcTPVTTAGAP 249
Cdd:COG3469 172 TTSASTTPSATTTATATTASGATTPSATTTATT-----TGPPTPGLP 213
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
331-459 6.77e-05

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: 44.53  E-value: 6.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 331 AQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSqQKELEDLLSPL 410
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALQKEI 98
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 24497607 411 EELVKEQSgtiylQHADEEREKTYKLaENIDAQLKRMAQDLKDIIEHLN 459
Cdd:COG1579  99 ESLKRRIS-----DLEDEILELMERI-EELEEELAELEAELAELEAELE 141
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
374-515 2.36e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 374 SLHREVEKVKLDQKRLDQELDFILSQQKELEDL-LSP--LEELVKEQSgtiYLQHADEEREKTYKLAE-------NIDAQ 443
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAaLQPgeEEELEEERR---RLSNAEKLREALQEALEalsggegGALDL 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 444 LKRMAQDLKDIIEHLNTSGAPADT----SDPLQQICKILNAHMDS-------LQWIDQ-NSAL--LQRK----VEEVTKV 505
Cdd:COG0497 246 LGQALRALERLAEYDPSLAELAERlesaLIELEEAASELRRYLDSlefdperLEEVEErLALLrrLARKygvtVEELLAY 325
                       170
                ....*....|
gi 24497607 506 CEGRRKEQER 515
Cdd:COG0497 326 AEELRAELAE 335
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
331-516 3.72e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    331 AQLESLINKWSLELEDQERhflQQATQVNAWDRTLiengEKITSLHREVEKVKLDQKRLDQELDfilSQQKELEDLLSPL 410
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEE---RLAKLEAEIDKLL----AEIEELEREIEEERKRRDKLTEEYA---ELKEELEDLRAEL 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    411 EELVKEqSGTIYLQHADEERE----------------KTYKLAENIDAQLKRMAQDLKDIIEHLNTSGAPADTSD----- 469
Cdd:TIGR02169  374 EEVDKE-FAETRDELKDYREKleklkreinelkreldRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleikk 452
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 24497607    470 ---PLQQICKILNAHMDSLQWIDQNSALLQRKVEEVTKvcEGRRKEQERS 516
Cdd:TIGR02169  453 qewKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR--ELAEAEAQAR 500
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
367-512 4.13e-04

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: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   367 ENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEELVKEqsgtiyLQHADEEREKTYKLAENIDAQLKR 446
Cdd:pfam13851  23 NNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEE------LRKQLENYEKDKQSLKNLKARLKV 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24497607   447 MAQDLKDI-IEHlntsgapadtsDPLQQICKILNAHMDSL------------QWIDQNSALLQRKVEEVTKVCEGRRKE 512
Cdd:pfam13851  97 LEKELKDLkWEH-----------EVLEQRFEKVERERDELydkfeaaiqdvqQKTGLKNLLLEKKLQALGETLEKKEAQ 164
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
330-457 7.24e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.89  E-value: 7.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 330 YAQLESLINKWSLELEDQERH--FLQQATQVNAW--DRTLIENGEKITSLHREVEKVKLDQKRLDQELDfilSQQKELED 405
Cdd:cd00176  88 WEELRELAEERRQRLEEALDLqqFFRDADDLEQWleEKEAALASEDLGKDLESVEELLKKHKELEEELE---AHEPRLKS 164
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 24497607 406 LLSPLEELVKEQsgtiylqHADEEREKTYKLAEnidaqLKRMAQDLKDIIEH 457
Cdd:cd00176 165 LNELAEELLEEG-------HPDADEEIEEKLEE-----LNERWEELLELAEE 204
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
331-458 7.93e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  331 AQLESLINKWSlELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPL 410
Cdd:PRK03918 200 KELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24497607  411 EELVKE-----QSGTIYLQhADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 458
Cdd:PRK03918 279 EEKVKElkelkEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
PHA03255 PHA03255
BDLF3; Provisional
93-243 3.40e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 39.12  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   93 GASKLNLSNTAATPAMANPSGFGLG-----SSNLTNAISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGFSFTGGSTAQ 167
Cdd:PHA03255  28 GSSTASAGNVTGTTAVTTPSPSASGpstnqSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  168 PSGFNIGSAGNSAQP--TAPATLPFTPATPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTS---SATTGLSLCTP 242
Cdd:PHA03255 108 AQNITATEAGTGTSTgvTSNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPTVPDErqpSLSYGLPLWTL 187

                 .
gi 24497607  243 V 243
Cdd:PHA03255 188 V 188
 
Name Accession Description Interval E-value
Nsp1_C pfam05064
Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region ...
328-429 2.71e-46

Nsp1-like C-terminal region; This family probably forms a coiled-coil. This important region of Nsp1 is involved in binding Nup82.


Pssm-ID: 461540 [Multi-domain]  Cd Length: 114  Bit Score: 157.47  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   328 MTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLL 407
Cdd:pfam05064  13 LKNKTLDDIINKWSTQLSKQSKEFETQAAKVNEWDRVLVENGDKISKLYSETLEAEQDQNRIDQQLDYVESQQDELESLL 92
                          90       100
                  ....*....|....*....|..
gi 24497607   408 SPLEELVKEQSGTIYLQHADEE 429
Cdd:pfam05064  93 DNYEEQLEELLGDITSQNSDEE 114
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
1-255 4.68e-09

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 58.91  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607     1 MSGFNFGGTGAPT----GGFTFGTAKTAtttpatgfsfSTSGTGGFNFGAPFQPATSTPSTGLFSLATQTPATQttgftf 76
Cdd:pfam15967   1 MSGFSFGGGPGSTatagGGFSFGAAAAS----------NPGSTGGFSFGTLGAAPAATATTTTATLGLGGGLFG------ 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    77 gtatlASGGTGFSLGigasklnlsNTAATPAMANPSGFGLGSSNLTNAisstvtssqgtAPTGFVFGPSTtsvaPATTSG 156
Cdd:pfam15967  65 -----QKPATGFTFG---------TPASSTAATGPTGLTLGTPAATTA-----------ASTGFSLGFNK----PAASAT 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   157 GFSFTGGSTAqPSGFNIGSAGNSAQPTAPATlPFTPATPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTSSATTG 236
Cdd:pfam15967 116 PFSLPASSTS-GGGLSLGSVLTSTAAQQGAT-GFTLNLGGTPATTTAVSTGLSLGSTLTSLGGSLFQNTNSTGLGQTTLG 193
                         250
                  ....*....|....*....
gi 24497607   237 LSLCTPVTTAGAPTAGTQG 255
Cdd:pfam15967 194 LTLLATSTAPVSAPAASEG 212
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
49-249 3.21e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 49.75  E-value: 3.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  49 QPATSTPSTGLFSLATQTPATQTTGFTFGTATLASGGTGFSLGIGASKLNLSNTAATPAMANPSGFGLGSSNLTNAISST 128
Cdd:COG3469  12 AGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 129 V------TSSQGTAPTGFVFGPSTTSVAPATTSGGFSFTGGSTAQPSGFNIGSAGNSAQPTAPATLPFTPATPAATTAGA 202
Cdd:COG3469  92 TsatlvaTSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTT 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24497607 203 TQPAAPTPTATITSTGPSLFASIATAPTSSATTglslcTPVTTAGAP 249
Cdd:COG3469 172 TTSASTTPSATTTATATTASGATTPSATTTATT-----TGPPTPGLP 213
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
331-459 6.77e-05

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: 44.53  E-value: 6.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 331 AQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSqQKELEDLLSPL 410
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALQKEI 98
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 24497607 411 EELVKEQSgtiylQHADEEREKTYKLaENIDAQLKRMAQDLKDIIEHLN 459
Cdd:COG1579  99 ESLKRRIS-----DLEDEILELMERI-EELEEELAELEAELAELEAELE 141
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
332-458 1.72e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 332 QLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDfilSQQKELEDLLSPLE 411
Cdd:COG4372  42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE---SLQEEAEELQEELE 118
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 24497607 412 ELVKEQSG-TIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 458
Cdd:COG4372 119 ELQKERQDlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
374-515 2.36e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 374 SLHREVEKVKLDQKRLDQELDFILSQQKELEDL-LSP--LEELVKEQSgtiYLQHADEEREKTYKLAE-------NIDAQ 443
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAaLQPgeEEELEEERR---RLSNAEKLREALQEALEalsggegGALDL 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 444 LKRMAQDLKDIIEHLNTSGAPADT----SDPLQQICKILNAHMDS-------LQWIDQ-NSAL--LQRK----VEEVTKV 505
Cdd:COG0497 246 LGQALRALERLAEYDPSLAELAERlesaLIELEEAASELRRYLDSlefdperLEEVEErLALLrrLARKygvtVEELLAY 325
                       170
                ....*....|
gi 24497607 506 CEGRRKEQER 515
Cdd:COG0497 326 AEELRAELAE 335
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
331-516 3.72e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    331 AQLESLINKWSLELEDQERhflQQATQVNAWDRTLiengEKITSLHREVEKVKLDQKRLDQELDfilSQQKELEDLLSPL 410
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEE---RLAKLEAEIDKLL----AEIEELEREIEEERKRRDKLTEEYA---ELKEELEDLRAEL 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    411 EELVKEqSGTIYLQHADEERE----------------KTYKLAENIDAQLKRMAQDLKDIIEHLNTSGAPADTSD----- 469
Cdd:TIGR02169  374 EEVDKE-FAETRDELKDYREKleklkreinelkreldRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleikk 452
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 24497607    470 ---PLQQICKILNAHMDSLQWIDQNSALLQRKVEEVTKvcEGRRKEQERS 516
Cdd:TIGR02169  453 qewKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR--ELAEAEAQAR 500
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
367-512 4.13e-04

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: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   367 ENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEELVKEqsgtiyLQHADEEREKTYKLAENIDAQLKR 446
Cdd:pfam13851  23 NNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEE------LRKQLENYEKDKQSLKNLKARLKV 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24497607   447 MAQDLKDI-IEHlntsgapadtsDPLQQICKILNAHMDSL------------QWIDQNSALLQRKVEEVTKVCEGRRKE 512
Cdd:pfam13851  97 LEKELKDLkWEH-----------EVLEQRFEKVERERDELydkfeaaiqdvqQKTGLKNLLLEKKLQALGETLEKKEAQ 164
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
343-489 4.51e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 343 ELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEELVKEqsgtiy 422
Cdd:COG4372  67 ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE------ 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24497607 423 LQHADEEREKTyklAENIDAQLKRMAQDLKDiIEHLNTSGAPADTSDPLQQICKILNAHMDSLQWID 489
Cdd:COG4372 141 LQSEIAEREEE---LKELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
82-266 6.67e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 42.43  E-value: 6.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  82 ASGGTGFSLGIGASKLNLSNTAATPAMANPSGFGLGSSNLTNAISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGFSFT 161
Cdd:COG3469  15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 162 GGSTAQPSGFNIGSAGNSAQPTAPATLPFTPATPAATTAGATQPAAPTPTATITSTGPS---LFASIATAPTSSATTGLS 238
Cdd:COG3469  95 TLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVsgtETATGGTTTTSTTTTTTS 174
                       170       180
                ....*....|....*....|....*...
gi 24497607 239 LCTPVTTAGAPTAGTqgfslkAPGAASG 266
Cdd:COG3469 175 ASTTPSATTTATATT------ASGATTP 196
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
330-457 7.24e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.89  E-value: 7.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 330 YAQLESLINKWSLELEDQERH--FLQQATQVNAW--DRTLIENGEKITSLHREVEKVKLDQKRLDQELDfilSQQKELED 405
Cdd:cd00176  88 WEELRELAEERRQRLEEALDLqqFFRDADDLEQWleEKEAALASEDLGKDLESVEELLKKHKELEEELE---AHEPRLKS 164
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 24497607 406 LLSPLEELVKEQsgtiylqHADEEREKTYKLAEnidaqLKRMAQDLKDIIEH 457
Cdd:cd00176 165 LNELAEELLEEG-------HPDADEEIEEKLEE-----LNERWEELLELAEE 204
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
331-458 7.93e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  331 AQLESLINKWSlELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPL 410
Cdd:PRK03918 200 KELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24497607  411 EELVKE-----QSGTIYLQhADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL 458
Cdd:PRK03918 279 EEKVKElkelkEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
328-459 2.06e-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: 40.81  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    328 MTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELdfilsQQKELEDLL 407
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL-----EEAELKELQ 439
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24497607    408 SPLEELVKEQSGtiyLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLN 459
Cdd:TIGR02168  440 AELEELEEELEE---LQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
331-512 2.30e-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: 40.81  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    331 AQLESLINkwslELEDQERHFLQQA----------TQVNAWDRTLIenGEKITSLHREVEKVKLDQKRLDQELDFILSQQ 400
Cdd:TIGR02168  189 DRLEDILN----ELERQLKSLERQAekaerykelkAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAEL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    401 K-------ELEDLLSPLEELVKEQSGTIY------------LQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNTS 461
Cdd:TIGR02168  263 QeleekleELRLEVSELEEEIEELQKELYalaneisrleqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24497607    462 gapADTSDPLQQICKILNAHMDSLQWIDQNsalLQRKVEEVTKVCEGRRKE 512
Cdd:TIGR02168  343 ---EEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLRSK 387
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
101-261 2.39e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.67  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   101 NTAATPAMaNPSGFGlGSSNLTNAISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGFSFTGGSTAQPSGFNIGS---AG 177
Cdd:pfam05109 427 STTTSPTL-NTTGFA-APNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTeskAP 504
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   178 NSAQPTAPATLPftpatPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTSSATTGlslcTPVTTAGAPTAGTQGFS 257
Cdd:pfam05109 505 DMTSPTSAVTTP-----TPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSP----TPAVTTPTPNATIPTLG 575

                  ....
gi 24497607   258 LKAP 261
Cdd:pfam05109 576 KTSP 579
CENP-Q pfam13094
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ...
375-496 2.85e-03

CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.


Pssm-ID: 432970 [Multi-domain]  Cd Length: 159  Bit Score: 38.42  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   375 LHREVEKVKLDQKRLDQELDF--ILSQQKELEDLLSPL--------EELVKEQSGTI----YLQ--------HADEEREK 432
Cdd:pfam13094   1 LLRRLARLPFPPGGKEKVLDFekLLDRNKALEAQLSAElhslelleEEIEKEEALLEsdeeYLEeleknakaEARERKEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   433 TyKLAENIDAQLKRMAQDLKDIIEHLNTSGAPADTSDP-----LQQICKILNAHMDSLQ-----------WIDQNSALLQ 496
Cdd:pfam13094  81 L-KKEHPLLQEDDSGVLSLPELSSDLGLGDTDFSLFDPtldeeLLPLLEQLQKHLESMQgnlaqleglneAIERAYAALD 159
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
35-221 3.00e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 40.12  E-value: 3.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  35 STSGTGGFNFGAPFQPATSTPSTGLFSLATQTPATQTTGFTFGTATLASGGTGFSLGIGASKLNLSNTAATPAMANPSGF 114
Cdd:COG3469  19 AVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 115 GLGSSNLTN----AISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGFSFTGGSTAQPSGFNIG---SAGNSAQPTAPAT 187
Cdd:COG3469  99 TSTASGANTgtstVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGtttTSTTTTTTSASTT 178
                       170       180       190
                ....*....|....*....|....*....|....
gi 24497607 188 LPFTPATPAATTAGATQPAAPTPTATITSTGPSL 221
Cdd:COG3469 179 PSATTTATATTASGATTPSATTTATTTGPPTPGL 212
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
82-311 3.20e-03

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443962 [Multi-domain]  Cd Length: 641  Bit Score: 40.19  E-value: 3.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  82 ASGGTGFSLGIGASKLNLSNTAATPAMANPSGFGLGSSNLTNAISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGFSFT 161
Cdd:COG4935 320 GGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAG 399
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 162 GGSTAQPSGFNIGSAGNSAQPTAPATLPFTPATPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTSSATTGLSLCT 241
Cdd:COG4935 400 GVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASST 479
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607 242 PVTTAGAPTAGTQGFSLKAPGAASGTSTTTSTAATATATTTSSSSTTGFALNLKPLApagIPSNTAAAVT 311
Cdd:COG4935 480 TAAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVA---IPDNGPAGVT 546
PHA03255 PHA03255
BDLF3; Provisional
93-243 3.40e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 39.12  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   93 GASKLNLSNTAATPAMANPSGFGLG-----SSNLTNAISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGFSFTGGSTAQ 167
Cdd:PHA03255  28 GSSTASAGNVTGTTAVTTPSPSASGpstnqSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  168 PSGFNIGSAGNSAQP--TAPATLPFTPATPAATTAGATQPAAPTPTATITSTGPSLFASIATAPTS---SATTGLSLCTP 242
Cdd:PHA03255 108 AQNITATEAGTGTSTgvTSNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPTVPDErqpSLSYGLPLWTL 187

                 .
gi 24497607  243 V 243
Cdd:PHA03255 188 V 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
332-451 3.57e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607    332 QLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHR-------EVEKVKldqkrldQELDFILSQQKELE 404
Cdd:TIGR02168  941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaaieEYEELK-------ERYDFLTAQKEDLT 1013
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 24497607    405 DLLSPLEELVKEqsgtiylqhADEEREKTYKLA-ENIDAQLKRMAQDL 451
Cdd:TIGR02168 1014 EAKETLEEAIEE---------IDREARERFKDTfDQVNENFQRVFPKL 1052
PRK11901 PRK11901
hypothetical protein; Reviewed
93-261 4.80e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 39.28  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607   93 GASKLNLSNTAATPAMANPSGFGLGSSNLTNAISSTVTSSQGTAPTGFVFGPSTTSVAPATTSGGF-------SFTGGST 165
Cdd:PRK11901  75 AEKNIDLSGSSSLSSGNQSSPSAANNTSDGHDASGVKNTAPPQDISAPPISPTPTQAAPPQTPNGQqrielpgNISDALS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24497607  166 AQPSGFNIGSAG----NSAQPTAPATLPftpaTPAATTAGATQPAAPTPTATITSTGPslfasiATAPTSSATTGLSLCT 241
Cdd:PRK11901 155 QQQGQVNAASQNaqgnTSTLPTAPATVA----PSKGAKVPATAETHPTPPQKPATKKP------AVNHHKTATVAVPPAT 224
                        170       180
                 ....*....|....*....|
gi 24497607  242 PvtTAGAPTAGTQGFSLKAP 261
Cdd:PRK11901 225 S--GKPKSGAASARALSSAP 242
 
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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