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Conserved domains on  [gi|34534793|dbj|BAC87112|]
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unnamed protein product [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10573383)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  11179890|12665246|11361095|10940247
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 198-223 3.46e-09

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


:

Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 51.79  E-value: 3.46e-09
                          10        20
                  ....*....|....*....|....*.
gi 34534793   198 LYCPACDKSFKTEKAMKNHEKSKKHR 223
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
PTZ00121 super family cl31754
MAEBL; Provisional
 51-233 6.71e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793    51 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQlvafiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 130
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793   131 AKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKdsDEAEDAELYDDLYCPACDKSFKTE 210
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEA 1643

                         170       180
                  ....*....|....*....|...
gi 34534793   211 KAMKNHEKSKKHREMVALLKQQL 233
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEE 1666
 
Name Accession Description Interval E-value
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 198-223 3.46e-09

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 51.79  E-value: 3.46e-09
                          10        20
                  ....*....|....*....|....*.
gi 34534793   198 LYCPACDKSFKTEKAMKNHEKSKKHR 223
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 197-229 1.03e-06

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 44.94  E-value: 1.03e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 34534793    197 DLYCPACDKSFKTEKAMKNHEKSKKHREMVALL 229
Cdd:smart00451   3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
PTZ00121 PTZ00121
MAEBL; Provisional
 51-233 6.71e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793    51 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQlvafiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 130
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793   131 AKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKdsDEAEDAELYDDLYCPACDKSFKTE 210
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEA 1643

                         170       180
                  ....*....|....*....|...
gi 34534793   211 KAMKNHEKSKKHREMVALLKQQL 233
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEE 1666
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 32-151 9.91e-05

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 44.25  E-value: 9.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793  32 VHPFYAYWQSFCTQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQ 111
Cdd:COG5269 163 VEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ 238

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 34534793 112 nAEKARKAEEMRRQQKLKQAKLVEQYREQSWMTMANLEKE 151
Cdd:COG5269 239 -EKEMKKIRKWEREAGARLKALAALKGKAEAKNKAEIEAE 277
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 64-182 6.39e-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: 38.75  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793    64 EKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQswm 143
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--- 243

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 34534793   144 tMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEED 182
Cdd:pfam13868 244 -QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEA 281
 
Name Accession Description Interval E-value
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 198-223 3.46e-09

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 51.79  E-value: 3.46e-09
                          10        20
                  ....*....|....*....|....*.
gi 34534793   198 LYCPACDKSFKTEKAMKNHEKSKKHR 223
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 197-229 1.03e-06

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 44.94  E-value: 1.03e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 34534793    197 DLYCPACDKSFKTEKAMKNHEKSKKHREMVALL 229
Cdd:smart00451   3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
zf-met pfam12874
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ...
 198-222 1.71e-06

Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.


Pssm-ID: 463736 [Multi-domain]  Cd Length: 25  Bit Score: 44.02  E-value: 1.71e-06
                          10        20
                  ....*....|....*....|....*
gi 34534793   198 LYCPACDKSFKTEKAMKNHEKSKKH 222
Cdd:pfam12874   1 FYCELCNVTFNSESQLKSHLQGKKH 25
PTZ00121 PTZ00121
MAEBL; Provisional
 51-233 6.71e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793    51 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQlvafiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 130
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793   131 AKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKdsDEAEDAELYDDLYCPACDKSFKTE 210
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEA 1643

                         170       180
                  ....*....|....*....|...
gi 34534793   211 KAMKNHEKSKKHREMVALLKQQL 233
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEE 1666
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 32-151 9.91e-05

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 44.25  E-value: 9.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793  32 VHPFYAYWQSFCTQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQ 111
Cdd:COG5269 163 VEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ 238

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 34534793 112 nAEKARKAEEMRRQQKLKQAKLVEQYREQSWMTMANLEKE 151
Cdd:COG5269 239 -EKEMKKIRKWEREAGARLKALAALKGKAEAKNKAEIEAE 277
PTZ00121 PTZ00121
MAEBL; Provisional
 51-224 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793    51 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQ----- 125
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKveqlk 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793   126 ----QKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDE-----AEDAELYD 196
Cdd:PTZ00121 1640 kkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAE 1719

                         170       180
                  ....*....|....*....|....*...
gi 34534793   197 DLYCPACDKSFKTEKAMKNHEKSKKHRE 224
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
PTZ00121 PTZ00121
MAEBL; Provisional
 51-220 1.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793    51 KEEYDTRQASNRWEKRAMEKENKKIRDKARK----EKNELVRQLVAFIRKRD-------KRVQAHRKLVEEQNAEKARKA 119
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAEEARKAEDakrveiaRKAEDARKAEEARKAEDAKKA 1178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793   120 EEMRRQQKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDLY 199
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258

                         170       180
                  ....*....|....*....|.
gi 34534793   200 CPACDKSFKTEKAMKNHEKSK 220
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARK 1279
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 64-182 6.39e-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: 38.75  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793    64 EKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQswm 143
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--- 243

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 34534793   144 tMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEED 182
Cdd:pfam13868 244 -QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEA 281
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
66-198 6.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34534793   66 RAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ--AKLVEQYREQSWM 143
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEelAELLKELEELGFE 585

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 34534793  144 TMANLEKELQEMEARYEK--EFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDL 198
Cdd:PRK03918 586 SVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
 
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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